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1

Zhang, XiaoHong, YuJi Miao, XiaoDan Hu, Rui Min, PeiDang Liu, and HaiQian Zhang. "Gamma Radiation-Induced Damage in the Zinc Finger of the Transcription Factor IIIA." Bioinorganic Chemistry and Applications 2016 (2016): 1–7. http://dx.doi.org/10.1155/2016/1642064.

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A zinc finger motif is an element of proteins that can specifically recognize and bind to DNA. Because they contain multiple cysteine residues, zinc finger motifs possess redox properties. Ionizing radiation generates a variety of free radicals in organisms. Zinc finger motifs, therefore, may be a target of ionizing radiation. The effect of gamma radiation on the zinc finger motifs in transcription factor IIIA (TFIIIA), a zinc finger protein, was investigated. TFIIIA was exposed to different gamma doses from 60Co sources. The dose rates were 0.20 Gy/min and 800 Gy/h, respectively. The binding
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2

GREEN, Andrew, and Bibudhendra SARKAR. "Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition." Biochemical Journal 333, no. 1 (1998): 85–90. http://dx.doi.org/10.1042/bj3330085.

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Zinc fingers are among the major structural motifs found in proteins that are involved in eukaryotic gene regulation. Many of these zinc-finger domains are involved in DNA binding. This study investigated whether the zinc-co-ordinating (Cys)2(His)2 motif found in the three zinc fingers of zif268 could be replaced by a (Cys)4 motif while still preserving DNA recognition. (Cys)2(His)2-to-(Cys)4 mutations were generated in each of the three zinc fingers of zif268 individually, as well as in fingers 1 and 3, and fingers 2 and 3 together. Whereas finger 1 and finger 3 tolerate the switch, such an a
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3

MAURER-STROH, SEBASTIAN, HE GAO, HAO HAN, et al. "MOTIF DISCOVERY WITH DATA MINING IN 3D PROTEIN STRUCTURE DATABASES: DISCOVERY, VALIDATION AND PREDICTION OF THE U-SHAPE ZINC BINDING ("HUF-ZINC") MOTIF." Journal of Bioinformatics and Computational Biology 11, no. 01 (2013): 1340008. http://dx.doi.org/10.1142/s0219720013400088.

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Data mining in protein databases, derivatives from more fundamental protein 3D structure and sequence databases, has considerable unearthed potential for the discovery of sequence motif—structural motif—function relationships as the finding of the U-shape (Huf-Zinc) motif, originally a small student's project, exemplifies. The metal ion zinc is critically involved in universal biological processes, ranging from protein-DNA complexes and transcription regulation to enzymatic catalysis and metabolic pathways. Proteins have evolved a series of motifs to specifically recognize and bind zinc ions.
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4

Gebelein, Brian, and Raul Urrutia. "Sequence-Specific Transcriptional Repression by KS1, a Multiple-Zinc-Finger–Krüppel-Associated Box Protein." Molecular and Cellular Biology 21, no. 3 (2001): 928–39. http://dx.doi.org/10.1128/mcb.21.3.928-939.2001.

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ABSTRACT The vertebrate genome contains a large number of Krüppel-associated box–zinc finger genes that encode 10 or more C2-H2 zinc finger motifs. Members of this gene family have been proposed to function as transcription factors by binding DNA through their zinc finger region and repressing gene expression via the KRAB domain. To date, however, no Krüppel-associated box–zinc finger protein (KRAB-ZFP) and few proteins with 10 or more zinc finger motifs have been shown to bind DNA in a sequence-specific manner. Our laboratory has recently identified KS1, a member of the KRAB-ZFP family that
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5

Hasegawa, Atsushi, Hiroshi Kaneko, Daishi Ishihara, et al. "GATA1 Changes DNA-Binding Fashion in a Binding-Site-Specific Manner and Alters Transcriptional Activity during Erythropoiesis." Blood 126, no. 23 (2015): 3584. http://dx.doi.org/10.1182/blood.v126.23.3584.3584.

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Abstract GATA1 is a transcription factor that coordinately regulates multiple target genes during the development and differentiation of erythroid and megakaryocytic lineages through binding to GATA motif (A/T)GATA(A/G). GATA1 has four functional domains, i.e., two transactivation domains reside in amino- and carboxyl- terminus, which transactivate GATA1 target genes redundantly and/or cooperatively, and two zinc-finger domains in the middle of the protein. The two zinc finger domains of GATA1 have been characterized extensively and their links to human diseases have also been identified. Carb
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6

Parraga, G., L. Young, and R. E. Klevit. "Zinc-finger motifs and DNA binding." Trends in Biochemical Sciences 14, no. 10 (1989): 398. http://dx.doi.org/10.1016/0968-0004(89)90283-1.

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7

Gao, Xiang, Daniel J. Rowley, Xiaowu Gai, and Daniel F. Voytas. "Ty5 gag Mutations Increase Retrotransposition and Suggest a Role for Hydrogen Bonding in the Function of the Nucleocapsid Zinc Finger." Journal of Virology 76, no. 7 (2002): 3240–47. http://dx.doi.org/10.1128/jvi.76.7.3240-3247.2002.

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ABSTRACT The Ty5 retrotransposon of Saccharomyces paradoxus transposes in Saccharomyces cerevisiae at frequencies 1,000-fold lower than do the native Ty1 elements. The low transposition activity of Ty5 could be due to differences in cellular environments between these yeast species or to naturally occurring mutations in Ty5. By screening of a Ty5 mutant library, two single mutants (D252N and Y68C) were each found to increase transposition approximately sixfold. When combined, transposition increased 36-fold, implying that the two mutations act independently. Neither mutation affected Ty5 prote
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8

Bowzard, J. Bradford, Robert P. Bennett, Neel K. Krishna, Sandra M. Ernst, Alan Rein, and John W. Wills. "Importance of Basic Residues in the Nucleocapsid Sequence for Retrovirus Gag Assembly and Complementation Rescue." Journal of Virology 72, no. 11 (1998): 9034–44. http://dx.doi.org/10.1128/jvi.72.11.9034-9044.1998.

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ABSTRACT The Gag proteins of Rous sarcoma virus (RSV) and human immunodeficiency virus (HIV) contain small interaction (I) domains within their nucleocapsid (NC) sequences. These overlap the zinc finger motifs and function to provide the proper density to viral particles. There are two zinc fingers and at least two I domains within these Gag proteins. To more thoroughly characterize the important sequence features and properties of I domains, we analyzed Gag proteins that contain one or no zinc finger motifs. Chimeric proteins containing the amino-terminal half of RSV Gag and various portions
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9

Guo, Jianhui, Tiyun Wu, Bradley F. Kane, et al. "Subtle Alterations of the Native Zinc Finger Structures Have Dramatic Effects on the Nucleic Acid Chaperone Activity of Human Immunodeficiency Virus Type 1 Nucleocapsid Protein." Journal of Virology 76, no. 9 (2002): 4370–78. http://dx.doi.org/10.1128/jvi.76.9.4370-4378.2002.

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ABSTRACT The nucleocapsid protein (NC) of human immunodeficiency virus type 1 has two zinc fingers, each containing the invariant CCHC zinc-binding motif; however, the surrounding amino acid context is not identical in the two fingers. Recently, we demonstrated that zinc coordination is required when NC unfolds complex secondary structures in RNA and DNA minus- and plus-strand transfer intermediates; this property of NC reflects its nucleic acid chaperone activity. Here we have analyzed the chaperone activities of mutants having substitutions of alternative zinc-coordinating residues, i.e., CC
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10

Guo, Xuemin, John-William N. Carroll, Margaret R. MacDonald, Stephen P. Goff, and Guangxia Gao. "The Zinc Finger Antiviral Protein Directly Binds to Specific Viral mRNAs through the CCCH Zinc Finger Motifs." Journal of Virology 78, no. 23 (2004): 12781–87. http://dx.doi.org/10.1128/jvi.78.23.12781-12787.2004.

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ABSTRACT The zinc finger antiviral protein (ZAP) is a recently isolated host antiviral factor. It specifically inhibits the replication of Moloney murine leukemia virus (MLV) and Sindbis virus (SIN) by preventing the accumulation of viral RNA in the cytoplasm. For this report, we mapped the viral sequences that are sensitive to ZAP inhibition. The viral sequences were cloned into a luciferase reporter and analyzed for the ability to mediate ZAP-dependent destabilization of the reporter. The sensitive sequence in MLV was mapped to the 3′ long terminal repeat; the sensitive sequences in SIN were
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11

Tsai, Robert Y. L., and Randall R. Reed. "Identification of DNA Recognition Sequences and Protein Interaction Domains of the Multiple-Zn-Finger Protein Roaz." Molecular and Cellular Biology 18, no. 11 (1998): 6447–56. http://dx.doi.org/10.1128/mcb.18.11.6447.

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ABSTRACT Roaz, a rat C2H2 zinc finger protein, plays a role in the regulation of olfactory neuronal differentiation through its interaction with the Olf-1/EBF transcription factor family. An additional role for the Roaz/Olf-1/EBF heterodimeric protein is suggested by its ability to regulate gene activation at a distinct promoter lacking Olf-1/EBF-binding sites. Using an in vitro binding-site selection assay (Selex), we demonstrate that Roaz protein binds to novel inverted perfect or imperfect repeats of GCACCC separated by 2 bp. We show that Roaz is capable of binding to a canonical consensus
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12

Zhang, Jun-Wu, Han Peng, and Zhan-Wen Du. "Identification, Characterization of a Novel Zinc Finger Protein (HZF1) Gene and Its Roles in Erythroid Differentiation and Megakaryocyte Differentiation." Blood 106, no. 11 (2005): 4237. http://dx.doi.org/10.1182/blood.v106.11.4237.4237.

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Abstract A significant number of transcription factors contain evolutionarily conserved zinc finger motifs. The classical C2H2 zinc finger motif, which employs two cysteine and two histidine residues to coordinate a single zinc ion, is a maim type of the zinc finger proteins. Many of the identified C2H2 type zinc protein have been demonstrated to be transcription factors that play important roles in differentiation and development of cells and tissues of higher organisms. In this study, we obtained some novel expression sequence tags (ESTs) containing C2H2 type motifs by reverse transcription-
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13

Su, Dan, Zhiyong Lou, Fei Sun, et al. "Dodecamer Structure of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein nsp10." Journal of Virology 80, no. 16 (2006): 7902–8. http://dx.doi.org/10.1128/jvi.00483-06.

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ABSTRACT The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-Å resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)2-C-(X)5-H-(X)6-C and C-(X)2-C-(X)7-C-(X)-C. The nsp10 crystal structure is the f
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14

Rollins, M. B., S. Del Rio, A. L. Galey, D. R. Setzer, and M. T. Andrews. "Role of TFIIIA zinc fingers in vivo: analysis of single-finger function in developing Xenopus embryos." Molecular and Cellular Biology 13, no. 8 (1993): 4776–83. http://dx.doi.org/10.1128/mcb.13.8.4776-4783.1993.

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The Xenopus 5S RNA gene-specific transcription factor IIIA (TFIIIA) has nine consecutive Cys2His2 zinc finger motifs. Studies were conducted in vivo to determine the contribution of each of the nine zinc fingers to the activity of TFIIIA in living cells. Nine separate TFIIIA mutants were expressed in Xenopus embryos following microinjection of their respective in vitro-derived mRNAs. Each mutant contained a single histidine-to-asparagine substitution in the third zinc ligand position of an individual zinc finger. These mutations result in structural disruption of the mutated finger with little
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15

Rollins, M. B., S. Del Rio, A. L. Galey, D. R. Setzer, and M. T. Andrews. "Role of TFIIIA zinc fingers in vivo: analysis of single-finger function in developing Xenopus embryos." Molecular and Cellular Biology 13, no. 8 (1993): 4776–83. http://dx.doi.org/10.1128/mcb.13.8.4776.

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The Xenopus 5S RNA gene-specific transcription factor IIIA (TFIIIA) has nine consecutive Cys2His2 zinc finger motifs. Studies were conducted in vivo to determine the contribution of each of the nine zinc fingers to the activity of TFIIIA in living cells. Nine separate TFIIIA mutants were expressed in Xenopus embryos following microinjection of their respective in vitro-derived mRNAs. Each mutant contained a single histidine-to-asparagine substitution in the third zinc ligand position of an individual zinc finger. These mutations result in structural disruption of the mutated finger with little
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16

Chen, Yan, Stacy D. Carrington-Lawrence, Ping Bai, and Sandra K. Weller. "Mutations in the Putative Zinc-Binding Motif of UL52 Demonstrate a Complex Interdependence between the UL5 and UL52 Subunits of the Human Herpes Simplex Virus Type 1 Helicase/Primase Complex." Journal of Virology 79, no. 14 (2005): 9088–96. http://dx.doi.org/10.1128/jvi.79.14.9088-9096.2005.

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ABSTRACT Herpes simplex virus type 1 (HSV-1) encodes a heterotrimeric helicase-primase (UL5/8/52) complex. UL5 contains seven motifs found in helicase superfamily 1, and UL52 contains conserved motifs found in primases. The contributions of each subunit to the biochemical activities of the complex, however, remain unclear. We have previously demonstrated that a mutation in the putative zinc finger at UL52 C terminus abrogates not only primase but also ATPase, helicase, and DNA-binding activities of a UL5/UL52 subcomplex, indicating a complex interdependence between the two subunits. To test th
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17

Shastry, B. S. "Transcription factor IIIA (TFIIIA) in the second decade." Journal of Cell Science 109, no. 3 (1996): 535–39. http://dx.doi.org/10.1242/jcs.109.3.535.

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Transcription factor IIIA is a very extensively studied eukaryotic gene specific factor. It is a special member of the zinc finger family of nucleic acid binding proteins with multiple functions. Its N-terminal polypeptide (280 amino acid residue containing peptide; finger containing region) carries out sequence specific DNA and RNA binding and the C-terminal peptide (65 amino acid residue containing peptide; non-finger region) is involved in the transactivation process possibly by interacting with other general factors. It is a unique factor in the sense that it binds to two structurally diff
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18

Nakamura, Takuro, Yukari Yamazaki, Yuriko Saiki, et al. "Evi9 Encodes a Novel Zinc Finger Protein That Physically Interacts with BCL6, a Known Human B-Cell Proto-Oncogene Product." Molecular and Cellular Biology 20, no. 9 (2000): 3178–86. http://dx.doi.org/10.1128/mcb.20.9.3178-3186.2000.

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ABSTRACT Evi9 is a common site of retroviral integration in BXH2 murine myeloid leukemias. Here we show that Evi9 encodes a novel zinc finger protein with three tissue-specific isoforms: Evi9a (773 amino acids [aa]) contains two C2H2-type zinc finger motifs, a proline-rich region, and an acidic domain; Evi9b (486 aa) lacks the first zinc finger motif and part of the proline-rich region; Evi9c (239 aa) lacks all but the first zinc finger motif. Proviral integration sites are located in the first intron of the gene and lead to increased gene expression. Evi9a and Evi9c, but not Evi9b, show trans
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19

Franklin, A. J., T. L. Jetton, K. D. Shelton, and M. A. Magnuson. "BZP, a novel serum-responsive zinc finger protein that inhibits gene transcription." Molecular and Cellular Biology 14, no. 10 (1994): 6773–88. http://dx.doi.org/10.1128/mcb.14.10.6773-6788.1994.

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We report the fortuitous isolation of cDNA clones encoding a novel zinc finger DNA-binding protein termed BZP. The protein encoded is 114 kDa and contains eight zinc finger motifs, seven of which are present in two clusters at opposite ends of the molecule. Both finger clusters bound to the 9-bp sequence AAAGGTGCA with apparent Kds of approximately 2.5 nM. Two of the finger motifs within the amino- and carboxy-terminal finger clusters share 63% amino acid identity. BZP inhibited transcription of the herpes simplex virus thymidine kinase promoter when copies of the 9-bp target motif were linked
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20

Franklin, A. J., T. L. Jetton, K. D. Shelton, and M. A. Magnuson. "BZP, a novel serum-responsive zinc finger protein that inhibits gene transcription." Molecular and Cellular Biology 14, no. 10 (1994): 6773–88. http://dx.doi.org/10.1128/mcb.14.10.6773.

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We report the fortuitous isolation of cDNA clones encoding a novel zinc finger DNA-binding protein termed BZP. The protein encoded is 114 kDa and contains eight zinc finger motifs, seven of which are present in two clusters at opposite ends of the molecule. Both finger clusters bound to the 9-bp sequence AAAGGTGCA with apparent Kds of approximately 2.5 nM. Two of the finger motifs within the amino- and carboxy-terminal finger clusters share 63% amino acid identity. BZP inhibited transcription of the herpes simplex virus thymidine kinase promoter when copies of the 9-bp target motif were linked
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21

Kanakoglou, Dimitrios S., Andromachi Pampalou, Lina S. Malakou, et al. "Central Role of C2H2-Type Zinc Finger-Containing Genes in Pediatric Brain Tumors." DNA 2, no. 1 (2022): 1–21. http://dx.doi.org/10.3390/dna2010001.

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Zinc fingers consist of one of the most abundant motifs in transcription factors and DNA-binding proteins. Recent studies provide evidence on the pathological implication of zinc finger proteins in various neurodevelopmental disorders and malignancies but their role in pediatric brain tumors is largely unexplored. To this end, we investigated the differential expression of zinc finger-containing genes along with relevant biological processes and pathways among four main brain tumor categories (pilocytic astrocytomas, ependymomas, medulloblastomas and glioblastomas). By employing an extended bi
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22

Bragg, Jennifer N., Diane M. Lawrence та Andrew O. Jackson. "The N-Terminal 85 Amino Acids of the Barley Stripe Mosaic Virus γb Pathogenesis Protein Contain Three Zinc-Binding Motifs". Journal of Virology 78, № 14 (2004): 7379–91. http://dx.doi.org/10.1128/jvi.78.14.7379-7391.2004.

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ABSTRACT Barley stripe mosaic virus RNAγ encodes γb, a cysteine-rich protein that affects pathogenesis. Nine of the eleven cysteines are concentrated in two clusters, designated C1 (residues 1 to 23) and C2 (residues 60 to 85), that are arranged in zinc finger-like motifs. A basic motif (BM) rich in lysine and arginine (residues 19 to 47) resides between the C1 and C2 clusters. We have demonstrated that γb binds zinc and that the C1, BM, and C2 motifs have independent zinc-binding activities. To evaluate the requirements for binding, mutations were introduced into each region. Cysteine residue
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23

Popov, Sergei, Elena Popova, Michio Inoue, and Heinrich G. Göttlinger. "Human Immunodeficiency Virus Type 1 Gag Engages the Bro1 Domain of ALIX/AIP1 through the Nucleocapsid." Journal of Virology 82, no. 3 (2007): 1389–98. http://dx.doi.org/10.1128/jvi.01912-07.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) and other retroviruses harbor short peptide motifs in Gag that promote the release of infectious virions. These motifs, known as late assembly (L) domains, recruit a cellular budding machinery that is required for the formation of multivesicular bodies (MVBs). The primary L domain of HIV-1 maps to a PTAP motif in the p6 region of Gag and engages the MVB pathway by binding to Tsg101. Additionally, HIV-1 p6 harbors an auxiliary L domain that binds to the V domain of ALIX, another component of the MVB pathway. We now show that ALIX also binds t
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24

Smith, Alexander E. F., Farzin Farzaneh, and Kevin G. Ford. "Single zinc-finger extension: enhancing transcriptional activity and specificity of three-zinc-finger proteins." Biological Chemistry 386, no. 2 (2005): 95–99. http://dx.doi.org/10.1515/bc.2005.012.

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AbstractIn order to demonstrate that an existing zinc-finger protein can be simply modified to enhance DNA binding and sequence discrimination in both episomal and chromatin contexts using existing zinc-finger DNA recognition code data, and without recourse to phage display and selection strategies, we have examined the consequences of a single zinc-finger extension to a synthetic three-zinc-finger VP16 fusion protein, on transcriptional activation from model target promoters harbouring the zinc-finger binding sequences. We report a nearly 10-fold enhanced transcriptional activation by the fou
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25

Huang, Shih-Ming, Sheng-Ping Huang, Sung-Ling Wang та Pei-Yao Liu. "Importin α1 is involved in the nuclear localization of Zac1 and the induction of p21WAF1/CIP1 by Zac1". Biochemical Journal 402, № 2 (2007): 359–66. http://dx.doi.org/10.1042/bj20061295.

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Zac1, a novel seven-zinc-finger transcription factor, preferentially binds GC-rich DNA elements and has intrinsic transactivation activity. To date, the NLS (nuclear localization signal) of Zac1 has not been empirically determined. We generated a series of EGFP (enhanced green fluorescence protein)-tagged deletion mutants of Zac1 and examined their subcellular localization, from which we defined two NLSs within the DNA-binding (or zinc-finger) domain. Fusion proteins consisting of the two EGFP-tagged zinc-finger clusters (zinc finger motifs 1–3 and 4–7) were located exclusively in the nucleus,
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26

MORISAKI, Tatsuya, Miki IMANISHI, Shiroh FUTAKI, and Yukio SUGIURA. "Artificial Transcription Factors Based on Multi-zinc Finger Motifs." YAKUGAKU ZASSHI 130, no. 1 (2010): 45–48. http://dx.doi.org/10.1248/yakushi.130.45.

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Guo, Jianhui, Tiyun Wu, Jada Anderson, et al. "Zinc Finger Structures in the Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Facilitate Efficient Minus- and Plus-Strand Transfer." Journal of Virology 74, no. 19 (2000): 8980–88. http://dx.doi.org/10.1128/jvi.74.19.8980-8988.2000.

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ABSTRACT The nucleocapsid protein (NC) of human immunodeficiency virus type 1 (HIV-1) has two zinc fingers, each containing the invariant metal ion binding residues CCHC. Recent reports indicate that mutations in the CCHC motifs are deleterious for reverse transcription in vivo. To identify reverse transcriptase (RT) reactions affected by such changes, we have probed zinc finger functions in NC-dependent RT-catalyzed HIV-1 minus- and plus-strand transfer model systems. Our approach was to examine the activities of wild-type NC and a mutant in which all six cysteine residues were replaced by se
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28

Longworth, Michelle S., and Laimonis A. Laimins. "The Binding of Histone Deacetylases and the Integrity of Zinc Finger-Like Motifs of the E7 Protein Are Essential for the Life Cycle of Human Papillomavirus Type 31." Journal of Virology 78, no. 7 (2004): 3533–41. http://dx.doi.org/10.1128/jvi.78.7.3533-3541.2004.

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ABSTRACT The E7 oncoprotein of high-risk human papillomaviruses (HPVs) binds to and alters the action of cell cycle regulatory proteins such as members of the retinoblastoma (Rb) family of proteins as well as the histone deacetylases (HDACs). To examine the significance of the binding of E7 to HDACs in the viral life cycle, a mutational analysis of the E7 open reading frame was performed in the context of the complete HPV type 31 (HPV-31) genome. Human foreskin keratinocytes were transfected with wild-type HPV-31 genomes or HPV-31 genomes containing mutations in HDAC binding sequences as well
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Perkins, A. S., R. Fishel, N. A. Jenkins, and N. G. Copeland. "Evi-1, a murine zinc finger proto-oncogene, encodes a sequence-specific DNA-binding protein." Molecular and Cellular Biology 11, no. 5 (1991): 2665–74. http://dx.doi.org/10.1128/mcb.11.5.2665-2674.1991.

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Evi-1 was originally identified as a common site of viral integration in murine myeloid tumors. Evi-1 encodes a 120-kDa polypeptide containing 10 zinc finger motifs located in two domains 380 amino acids apart and an acidic domain located carboxy terminal to the second set of zinc fingers. These features suggest that Evi-1 is a site-specific DNA-binding protein involved in the regulation of RNA transcription. We have purified Evi-1 protein from E. coli and have employed a gel shift-polymerase chain reaction method using random oligonucleotides to identify a high-affinity binding site for Evi-1
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30

Perkins, A. S., R. Fishel, N. A. Jenkins, and N. G. Copeland. "Evi-1, a murine zinc finger proto-oncogene, encodes a sequence-specific DNA-binding protein." Molecular and Cellular Biology 11, no. 5 (1991): 2665–74. http://dx.doi.org/10.1128/mcb.11.5.2665.

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Evi-1 was originally identified as a common site of viral integration in murine myeloid tumors. Evi-1 encodes a 120-kDa polypeptide containing 10 zinc finger motifs located in two domains 380 amino acids apart and an acidic domain located carboxy terminal to the second set of zinc fingers. These features suggest that Evi-1 is a site-specific DNA-binding protein involved in the regulation of RNA transcription. We have purified Evi-1 protein from E. coli and have employed a gel shift-polymerase chain reaction method using random oligonucleotides to identify a high-affinity binding site for Evi-1
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31

Arranz, V., F. Harper, Y. Florentin, E. Puvion, M. Kress, and M. Ernoult-Lange. "Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains." Molecular and Cellular Biology 17, no. 4 (1997): 2116–26. http://dx.doi.org/10.1128/mcb.17.4.2116.

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The human and murine MOK2 ortholog genes that are preferentially expressed in brain and testis tissues encode two different Krüppel-like zinc finger proteins. In this paper, we show that the MOK2 proteins are mainly associated with nuclear ribonucleoprotein components, including the nucleoli and extranucleolar structures, and exhibit specific RNA homopolymer binding activities. Moreover, we have identified an identical 18-bp specific DNA binding sequence for both MOK2 proteins using a pool of random sequence oligonucleotides. The DNA binding domain is localized in the seven adjacent zinc finge
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32

Nakaseko, Yukinobu, David Neuhaus, Aaron Klug, and Daniela Rhodes. "Adjacent zinc-finger motifs in multiple zinc-finger peptides from SWI5 form structurally independent, flexibly linked domains." Journal of Molecular Biology 228, no. 2 (1992): 619–36. http://dx.doi.org/10.1016/0022-2836(92)90845-b.

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33

Quinlan, Kate G. R., Marco Nardini, Alexis Verger, et al. "Specific Recognition of ZNF217 and Other Zinc Finger Proteins at a Surface Groove of C-Terminal Binding Proteins." Molecular and Cellular Biology 26, no. 21 (2006): 8159–72. http://dx.doi.org/10.1128/mcb.00680-06.

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ABSTRACT Numerous transcription factors recruit C-terminal binding protein (CtBP) corepressors. We show that the large zinc finger protein ZNF217 contacts CtBP. ZNF217 is encoded by an oncogene frequently amplified in tumors. ZNF217 contains a typical Pro-X-Asp-Leu-Ser (PXDLS) motif that binds in CtBP's PXDLS-binding cleft. However, ZNF217 also contains a second motif, Arg-Arg-Thr (RRT), that binds a separate surface on CtBP. The crystal structure of CtBP bound to an RRTGAPPAL peptide shows that it contacts a surface crevice distinct from the PXDLS binding cleft. Interestingly, both PXDLS and
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34

Yang, Chang, Rui Hao, Yong Fei Lan, et al. "Integrity of zinc finger motifs in PML protein is necessary for inducing its degradation by antimony." Metallomics 11, no. 8 (2019): 1419–29. http://dx.doi.org/10.1039/c9mt00102f.

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35

Heras, Sara R., M. Carmen Thomas, Francisco Macias, Manuel E. Patarroyo, Carlos Alonso, and Manuel C. López. "Nucleic-acid-binding properties of the C2-L1Tc nucleic acid chaperone encoded by L1Tc retrotransposon." Biochemical Journal 424, no. 3 (2009): 479–90. http://dx.doi.org/10.1042/bj20090766.

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It has been reported previously that the C2-L1Tc protein located in the Trypanosoma cruzi LINE (long interspersed nuclear element) L1Tc 3′ terminal end has NAC (nucleic acid chaperone) activity, an essential activity for retrotransposition of LINE-1. The C2-L1Tc protein contains two cysteine motifs of a C2H2 type, similar to those present in TFIIIA (transcription factor IIIA). The cysteine motifs are flanked by positively charged amino acid regions. The results of the present study show that the C2-L1Tc recombinant protein has at least a 16-fold higher affinity for single-stranded than for dou
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36

Okabe, Shinichiro, Tetsuya Fukuda, Kazuki Ishibashi, et al. "BAZF, a Novel Bcl6 Homolog, Functions as a Transcriptional Repressor." Molecular and Cellular Biology 18, no. 7 (1998): 4235–44. http://dx.doi.org/10.1128/mcb.18.7.4235.

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ABSTRACT The BCL6 gene, which has been identified from the chromosomal translocation breakpoint in B-cell lymphomas, functions as a sequence-specific transcriptional repressor. We cloned a novelBcl6-homologous gene, BAZF (encoding Bcl6-associated zinc finger protein). The predicted amino acid sequence of BAZF indicated that the BTB/POZ domain and the five repeats of the Krüppel-like zinc finger motif are located in the NH2-terminal region and the COOH-terminal region, respectively. BAZF associated with Bcl6 at the BTB/POZ domain and localized in the nucleus. Since zinc finger motifs of BAZF w
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37

MacPherson, Sarah, Marc Larochelle, and Bernard Turcotte. "A Fungal Family of Transcriptional Regulators: the Zinc Cluster Proteins." Microbiology and Molecular Biology Reviews 70, no. 3 (2006): 583–604. http://dx.doi.org/10.1128/mmbr.00015-06.

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SUMMARY The trace element zinc is required for proper functioning of a large number of proteins, including various enzymes. However, most zinc-containing proteins are transcription factors capable of binding DNA and are named zinc finger proteins. They form one of the largest families of transcriptional regulators and are categorized into various classes according to zinc-binding motifs. This review focuses on one class of zinc finger proteins called zinc cluster (or binuclear) proteins. Members of this family are exclusively fungal and possess the well-conserved motif CysX2CysX6CysX5-12CysX2C
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38

Kim, Min-Kyu, Lei Zhao, Soyoung Jeong, et al. "Structural and Biochemical Characterization of Thioredoxin-2 from Deinococcus radiodurans." Antioxidants 10, no. 11 (2021): 1843. http://dx.doi.org/10.3390/antiox10111843.

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Thioredoxin (Trx), a ubiquitous protein showing disulfide reductase activity, plays critical roles in cellular redox control and oxidative stress response. Trx is a member of the Trx system, comprising Trx, Trx reductase (TrxR), and a cognate reductant (generally reduced nicotinamide adenine dinucleotide phosphate, NADPH). Bacterial Trx1 contains only the Trx-fold domain, in which the active site CXXC motif that is critical for the disulfide reduction activity is located. Bacterial Trx2 contains an N-terminal extension, which forms a zinc-finger domain, including two additional CXXC motifs. Th
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39

Lee, Sang-Jin, Jae-Rin Lee, Hwa-Sun Hah, et al. "PIAS1 interacts with the KRAB zinc finger protein, ZNF133, via zinc finger motifs and regulates its transcriptional activity." Experimental & Molecular Medicine 39, no. 4 (2007): 450–57. http://dx.doi.org/10.1038/emm.2007.49.

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40

Chen, Canbin, Fangfang Xie, Kamran Shah, et al. "Genome-Wide Identification of WRKY Gene Family in Pitaya Reveals the Involvement of HmoWRKY42 in Betalain Biosynthesis." International Journal of Molecular Sciences 23, no. 18 (2022): 10568. http://dx.doi.org/10.3390/ijms231810568.

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The WRKY gene family is a plant-specific transcription factor (TF) that regulates many physiological processes and (a) biotic stress responses. Despite this, little is known about the molecular properties and roles of WRKY TFs in pitaya betalain biosynthesis. Here we report the identification of 70 WRKY in Hylocereus undatus, their gene structure, locations on each chromosome, systematic phylogenetic analysis, conserved motif analysis, and synteny of HuWRKY genes. HmoWRKY42 is a Group IIb WRKY protein and contains a coiled-coil motif, a WRKY domain and a C2H2 zinc-finger motif (CX5CX23HXH). Re
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41

Hudson, Nicholas O., and Bethany A. Buck-Koehntop. "Zinc Finger Readers of Methylated DNA." Molecules 23, no. 10 (2018): 2555. http://dx.doi.org/10.3390/molecules23102555.

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DNA methylation is a prevalent epigenetic modification involved in regulating a number of essential cellular processes, including genomic accessibility and transcriptional outcomes. As such, aberrant alterations in global DNA methylation patterns have been associated with a growing number of disease conditions. Nevertheless, the full mechanisms by which DNA methylation information is interpreted and translated into genomic responses is not yet fully understood. Methyl-CpG binding proteins (MBPs) function as important mediators of this essential process by selectively reading DNA methylation si
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42

Kato, N., K. Shimotohno, D. VanLeeuwen, and M. Cohen. "Human proviral mRNAs down regulated in choriocarcinoma encode a zinc finger protein related to Krüppel." Molecular and Cellular Biology 10, no. 8 (1990): 4401–5. http://dx.doi.org/10.1128/mcb.10.8.4401-4405.1990.

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RNA transcripts of the HERV-R (ERV3) human provirus that are abundant in placenta but absent in choriocarcinoma contain nonproviral genomic sequences at their 3' ends. We report here the isolation of cDNA clones of these genomic sequences. The transcripts encode a Krüppel-related zinc finger protein consisting of a unique leader region and more than 12 28-amino-acid finger motifs.
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43

Kato, N., K. Shimotohno, D. VanLeeuwen, and M. Cohen. "Human proviral mRNAs down regulated in choriocarcinoma encode a zinc finger protein related to Krüppel." Molecular and Cellular Biology 10, no. 8 (1990): 4401–5. http://dx.doi.org/10.1128/mcb.10.8.4401.

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RNA transcripts of the HERV-R (ERV3) human provirus that are abundant in placenta but absent in choriocarcinoma contain nonproviral genomic sequences at their 3' ends. We report here the isolation of cDNA clones of these genomic sequences. The transcripts encode a Krüppel-related zinc finger protein consisting of a unique leader region and more than 12 28-amino-acid finger motifs.
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44

Wang, S. S., D. R. Stanford, C. D. Silvers, and A. K. Hopper. "STP1, a gene involved in pre-tRNA processing, encodes a nuclear protein containing zinc finger motifs." Molecular and Cellular Biology 12, no. 6 (1992): 2633–43. http://dx.doi.org/10.1128/mcb.12.6.2633-2643.1992.

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STP1 is an unessential yeast gene involved in the removal of intervening sequences from some, but not all, families of intervening sequence-containing pre-tRNAs. Previously, we proposed that STP1 might encode a product that generates pre-tRNA conformations efficiently recognized by tRNA-splicing endonuclease. To test the predictions of this model, we have undertaken a molecular analysis of the STP1 gene and its products. The STP1 locus is located on chromosome IV close to at least two other genes involved in RNA splicing: PRP3 and SPP41. The STP1 open reading frame (ORF) could encode a peptide
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45

Wang, S. S., D. R. Stanford, C. D. Silvers, and A. K. Hopper. "STP1, a gene involved in pre-tRNA processing, encodes a nuclear protein containing zinc finger motifs." Molecular and Cellular Biology 12, no. 6 (1992): 2633–43. http://dx.doi.org/10.1128/mcb.12.6.2633.

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STP1 is an unessential yeast gene involved in the removal of intervening sequences from some, but not all, families of intervening sequence-containing pre-tRNAs. Previously, we proposed that STP1 might encode a product that generates pre-tRNA conformations efficiently recognized by tRNA-splicing endonuclease. To test the predictions of this model, we have undertaken a molecular analysis of the STP1 gene and its products. The STP1 locus is located on chromosome IV close to at least two other genes involved in RNA splicing: PRP3 and SPP41. The STP1 open reading frame (ORF) could encode a peptide
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46

Hasegawa, Atsushi, Hiroshi Kaneko, Daishi Ishihara, et al. "GATA1 Binding Kinetics on Conformation-Specific Binding Sites Elicit Differential Transcriptional Regulation." Molecular and Cellular Biology 36, no. 16 (2016): 2151–67. http://dx.doi.org/10.1128/mcb.00017-16.

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GATA1 organizes erythroid and megakaryocytic differentiation by orchestrating the expression of multiple genes that show diversified expression profiles. Here, we demonstrate that GATA1 monovalently binds to a single GATA motif (Single-GATA) while a monomeric GATA1 and a homodimeric GATA1 bivalently bind to two GATA motifs in palindromic (Pal-GATA) and direct-repeat (Tandem-GATA) arrangements, respectively, and form higher stoichiometric complexes on respective elements. The amino-terminal zinc (N) finger of GATA1 critically contributes to high occupancy of GATA1 on Pal-GATA. GATA1 lacking the
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47

Diaz, Brenda, Christopher Mederos, Kemin Tan, and Yuk-Ching Tse-Dinh. "Microbial Type IA Topoisomerase C-Terminal Domain Sequence Motifs, Distribution and Combination." International Journal of Molecular Sciences 23, no. 15 (2022): 8709. http://dx.doi.org/10.3390/ijms23158709.

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Type IA topoisomerases have highly conserved catalytic N-terminal domains for the cleaving and rejoining of a single DNA/RNA strand that have been extensively characterized. In contrast, the C-terminal region has been less covered. Two major types of small tandem C-terminal domains, Topo_C_ZnRpt (containing C4 zinc finger) and Topo_C_Rpt (without cysteines) were initially identified in Escherichia coli and Mycobacterium tuberculosis topoisomerase I, respectively. Their structures and interaction with DNA oligonucleotides have been revealed in structural studies. Here, we first present the dive
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48

Trainor, C. D., J. G. Omichinski, T. L. Vandergon, A. M. Gronenborn, G. M. Clore, and G. Felsenfeld. "A palindromic regulatory site within vertebrate GATA-1 promoters requires both zinc fingers of the GATA-1 DNA-binding domain for high-affinity interaction." Molecular and Cellular Biology 16, no. 5 (1996): 2238–47. http://dx.doi.org/10.1128/mcb.16.5.2238.

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GATA-1, a transcription factor essential for the development of the erythroid lineage, contains two adjacent highly conserved zinc finger motifs. The carboxy-terminal finger is necessary and sufficient for specific binding to the consensus GATA recognition sequence: mutant proteins containing only the amino-terminal finger do not bind. Here we identify a DNA sequence (GATApal) for which the GATA-1 amino-terminal finger makes a critical contribution to the strength of binding. The site occurs in the GATA-1 gene promoters of chickens, mice, and humans but occurs very infrequently in other verteb
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49

Rodriguez, Alyssa A., Jessica L. Wojtaszek, Briana H. Greer, et al. "An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3." Journal of Biological Chemistry 295, no. 46 (2020): 15566–75. http://dx.doi.org/10.1074/jbc.ra120.015541.

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The NEIL3 DNA glycosylase maintains genome integrity during replication by excising oxidized bases from single-stranded DNA (ssDNA) and unhooking interstrand cross-links (ICLs) at fork structures. In addition to its N-terminal catalytic glycosylase domain, NEIL3 contains two tandem C-terminal GRF-type zinc fingers that are absent in the other NEIL paralogs. ssDNA binding by the GRF–ZF motifs helps recruit NEIL3 to replication forks converged at an ICL, but the nature of DNA binding and the effect of the GRF–ZF domain on catalysis of base excision and ICL unhooking is unknown. Here, we show tha
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50

Bellini, M., J. C. Lacroix, and J. G. Gall. "A zinc-binding domain is required for targeting the maternal nuclear protein PwA33 to lampbrush chromosome loops." Journal of Cell Biology 131, no. 3 (1995): 563–70. http://dx.doi.org/10.1083/jcb.131.3.563.

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In oocytes of the newt Pleurodeles waltl, the maternal nuclear protein PwA33 occurs on the lampbrush chromosomes and in some nucleoplasmic particles of the germinal vesicle. PwA33 is a modular protein and we used site-directed mutagenesis to alter the sequences encoding two metal-binding regions, the C3HC4 (or RING finger) and B-box motifs. Several mutant clones were generated and their synthetic transcripts were injected into Pleurodeles oocytes for in vivo analysis. In the oocyte, all translation products localized in the germinal vesicle. Proteins encoded by RING finger mutant clones were d
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