Дисертації з теми "L11 Ribosomal Protein"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-26 дисертацій для дослідження на тему "L11 Ribosomal Protein".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте дисертації для різних дисциплін та оформлюйте правильно вашу бібліографію.
Jenvert, Rose-Marie. "The ribosome, stringent factor and the bacterial stringent response." Doctoral thesis, Stockholm : Wenner-Gren Institute for Experimental Biology, Stockholm University, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-6739.
Повний текст джерелаBouakaz, Lamine. "Versatile Implementations of an Improved Cell-Free System for Protein Biosynthesis : Functional and structural studies of ribosomal protein L11 and class II release factor RF3. Novel biotechnological approach for continuous protein biosynthesis." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Universitetsbiblioteket [distributör], 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-6325.
Повний текст джерелаGilkes, Daniele M. "Multiple modes of MDMX regulation affect p53 activation." [Tampa, Fla.] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002312.
Повний текст джерелаPetrov, Alexey. "Wiring the ribosome: functions of ribosomal proteins L3 and L10, and 5S rRNA." College Park, Md. : University of Maryland, 2006. http://hdl.handle.net/1903/4082.
Повний текст джерелаThesis research directed by: Cell Biology & Molecular Genetics. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
Mandava, Chandra Sekhar. "Ribosomal Stalk Protein L12 : Structure, Function and Application." Doctoral thesis, Uppsala universitet, Struktur- och molekylärbiologi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-157198.
Повний текст джерелаSimmons, Mary Kecia Rigsby. "Genetic characterization of ribosomal protein L10 in Saccharomyces cerevisiae." College Park, Md. : University of Maryland, 2005. http://hdl.handle.net/1903/2659.
Повний текст джерелаThesis research directed by: Cell Biology & Molecular Genetics. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
Pereira, Larissa Miranda. "Clonagem, expressão, purificação e caracterização estrutural da proteína ribossomal L10 humana recombinante." Universidade de São Paulo, 2009. http://www.teses.usp.br/teses/disponiveis/85/85131/tde-22092011-101810/.
Повний текст джерелаThe ribosomal protein L10 (RP L10) is a strong candidate to be included in the class of tumor suppressor proteins. This protein, also denominated as QM, is known to participate in the binding of ribosomal subunits 60S and 40S and the translation of mRNAs. It has a molecular weight that varies between 24 and 26 kDa and an isoelectric point of (pI) 10.5. The sequence of the protein QM is highly conserved in mammals, plants, invertebrates, insects and yeast which indicates its critical functions in a cell. As a tumor suppressor, RP L10 has been studied in strains of Wilm\'s tumor (WT-1) and tumor cells in the stomach, where was observed a decrease in the amount of its mRNA. More recently, the RP L10 was found in low amounts in the early stages of prostate adenoma and showed some mutation in ovarian cancer, what indicates its role as a suppressor protein in the development of these diseases. It has also been described that this protein interacts with c-Jun and c-Yes inhibiting growth factors and consequently, cell division. This work has an important role on the establishment of soluble expression of QM to give base information for further studies on expression that aim to evaluate the specific regions where it acts binding the 60S and 40S ribossomal subunits and translation, as well as its binding to proto-oncogenes. The cDNA for QM protein was amplified by PCR and cloned into periplasmic expression vector p3SN8. The QM protein was expressed in E. coli BL21 (DE3) in the region of cytoplasm and periplasm, the best condition was obtained from the expression of the recombinant plasmid QM p1813_QM at 25°C or 30°C, the soluble protein was obtained with small amounts of contaminants. The assays of secondary structure showed that the QM protein is predominantly alpha-helix, but when it loses the folding, this condition changes and the protein is replaced by β- sheet feature.
Burnett, Tracey A. "Analysis of the novel surface protein P159 and the ribosomal protein L7/L12 of mycoplasma hyopneumoniae." Access electronically, 2005. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20051104.145934/index.html.
Повний текст джерелаSimoff, Ivailo. "Ribosomal proteins L5 and L15 : Functional characterisation of important features, in vivo." Doctoral thesis, Stockholms universitet, Wenner-Grens institut, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-27731.
Повний текст джерелаFu, Yang. "Identification and Characterization of Novel Ribosomal Protein-binding RNA motifs in Bacteria." Thesis, Boston College, 2014. http://hdl.handle.net/2345/3795.
Повний текст джерелаAs the factory responsible for producing proteins, ribosomes are of great importance. In bacteria, ribosomes are composed of three ribosomal RNAs (rRNA) of different sizes, and around 50 ribosomal proteins (r-protein). During ribosome biogenesis in bacteria, synthesis of rRNAs and r-proteins are both tightly regulated and coordinated to ensure robust growth. In particular, a group of cis-regulatory RNA elements located in the 5' untranslated regions or the intergenic regions in r-protein operons are responsible for the regulation of r-protein biosynthesis. Based on the fact that RNA-regulated r-protein biosynthesis is essential and universal in bacteria, such unique and varied regulatory RNAs could provide new targets for antibacterial purpose. In this thesis, we report and experimentally verify a novel r-protein L1 regulation model that contains dual L1-binding RNA motif, and for the first time, a S6:S18 dimer-binding RNA structure in the S6 operon. We also describe Escherichia coli-based and Schizosaccharomyces pombe-based reporter systems for in vivo characterization of RNA-protein interactions. So far, both in vivo systems failed to report RNA-protein interactions, and thus need further tuning. In addition, we performed phage-display to select for regulatory RNA-binding small peptides and examined their effects on bacteria viability. One selected peptide, N-TVNFKLY-C, caused defective growth when overexpressed in E. coli. Yet, further studies must be conducted to verify the possibility that bacteria were killed by direct RNA-peptide interaction that disrupted the native r-protein regulation
Thesis (MS) — Boston College, 2014
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Biology
PEREIRA, LARISSA M. "Clonagem, expressao, purificacao e caracterizacao estrutural da proteina ribossomal L10 humana recombinante." reponame:Repositório Institucional do IPEN, 2009. http://repositorio.ipen.br:8080/xmlui/handle/123456789/9478.
Повний текст джерелаMade available in DSpace on 2014-10-09T13:57:22Z (GMT). No. of bitstreams: 0
Dissertacao (Mestrado)
IPEN/D
Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP
Klyashtornyy, Vladislav. "Principles of protein nucleic acid : recognition on the examples of the ribosomal protein L1 and the cold shock domain of YB-1 protein." Thesis, Evry-Val d'Essonne, 2012. http://www.theses.fr/2011EVRY0039/document.
Повний текст джерелаThis thesis is a structural study on the interaction between two model proteins and nucleic acids: the L1 protein (shuttle ribosome/mRNA) and the CSD subdomain of YB-1, a protein that regulates transcription and translation. Two methods are used: i) X-ray diffraction by crystals of L1:ribosomal or messenger RNA complexes and ii) molecular modeling and dynamics for the CSD interaction with homo-ribo or homo-deoxyribo- single-stranded nucleotide. The methods are described with their strengths and limitations. Results on L1-rARN/ARN enlighten the mechanisms regulating translation by showing differences in affinity for RNA of the subdomains I and II of L1. Analyses of L1 mutants in the RNA binding site from the subdomain I illuminate the nature of non-covalent bonds subtending the affinity of this subdomain for RNA and stress the importance of the structure of L1, its "complementarity" with RNA and of hydrogen bonds not accessible to the solvent. Molecular modeling and dynamics of the CSD:nucleic acids interaction shows that the nucleotide sequence modulates the affinity of the complex, oligoG giving the most stable complex followed by oligoU and then oligoA or oligoT and oligoC. The orientation of the RNA strand relative to the CSD also impacts the stability of the complex. An analysis of the interaction surfaces and of the nature of intermolecular bonds, shows that similar principles guide the L1: RNA and CSD: nucleic acids interactions, i.e. a complementary geometry between partners and presence of hydrogen bonds protected from the solvent
Vanet, Anne. "Etude de l'expression et de la fonction d'une methyltransferase modifiant une proteine particuliere (l11), du ribosome d'escherichia coli." Paris 7, 1994. http://www.theses.fr/1994PA077101.
Повний текст джерелаElhag, Gasmalla Abdelwahab. "Molecular characterization of full-length cDNAs for nuclear-encoded chloroplast ribosomal proteins L12, L24 and L27 of Nicotiana tabacum." Diss., The University of Arizona, 1991. http://hdl.handle.net/10150/185581.
Повний текст джерелаWillumeit, Regine. "Lokalisierung der Proteine L1, S6 und S10 des E.-coli-Ribosoms mit spinabhängiger Neutronenkleinwinkelstreuung /." Geesthacht : GKSS, 1996. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=007390140&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.
Повний текст джерелаGAUVIN, SEGANTIN SYLVIANE. "Expression du gene rpl21 codant pour la proteine l21 du ribosome plastidiale de l'epinard : etude de deux elements du promoteur." Université Joseph Fourier (Grenoble), 1996. http://www.theses.fr/1996GRE10213.
Повний текст джерелаSanejouand, Yves-Henri. "Etude theorique des mouvements internes de grande amplitude de la decaalanine et du fragment c-terminal de la proteine ribosomale l7/l12." Paris 11, 1990. http://www.theses.fr/1990PA112136.
Повний текст джерелаGopinathan, Lakshmi Vanden Heuvel John P. "Regulation of Peroxisome proliferator-activated receptor [alpha] by Ribosomal protein L11, murine double minute 2, and E6-associated protein." 2008. http://etda.libraries.psu.edu/theses/approved/WorldWideIndex/ETD-3573/index.html.
Повний текст джерелаHuang, Shuo-Yen, and 黃碩彥. "Interactions between Ribosomal Proteins and Endoplasmic Reticulum (ER): The role of large subunit ribosomal proptein L19 in making rough ER and ribosome assembly." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/51579057066224244798.
Повний текст джерела國立陽明大學
遺傳學研究所
91
During the process of protein translocation, the nascent polypeptide chain is recognized by signal recognition particles (SRP) which carry the ribosome-nascent polypeptide complex (RNC) to reside on the ER membrane. In the previous studies, our laboratory has found that human large subunit ribosomal protein L7 specifically bound to the ER membrane. This thesis is focused on the finding of another contact point from ribosome to the ER. Based on the 2.4-angstrom high-resolution structure of Archaea (Haloarcula marismortui) 50S ribosome, and the data of cryo-EM reconstitution of eukaryotic RNC-Sec61 complex structure, human ribosomal protein L19 has tentatively been suggested as one of the contact points from ribosome to ER. Thus, in this thesis, L19 was cloned and expressed in both prokaryotic and eukaryotic expression vectors. As the result shown, we have confirmed that L19 also has the ability to bind ER. We also found that recombinant L19 has made into ribosome assembly in 293T cell. During the process, we observed that L19 was co-localized with L7 in forming of the nuclear body-like microbodies outside the nucleoli. The observations predicted that the nuclear body-like microbodies may be a precursor of ribosome assembly. In the last part of this thesis, we have made a recombinant ribosome-containing modified L19 protein which carried a heart muscle kinase (HMK) recognition sequence (RRASV) at the C-terminal end of L19 protein. We examined whether this recombinant ribosome is able to be detected by kinase reaction or not, and the result was negative, suggesting that the C-terminal end of L19 is not exposed on surface.
Chi, Hsiao-Lan, and 紀筱嵐. "Nuclear Import of Eukaryotic Ribosomal Proteins: Cellular trafficking of human ribosomal protein L10 between the cell nucleus and the plasma membrane." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/89076727203258272443.
Повний текст джерела國立陽明大學
生命科學暨基因體科學研究所
95
In the eukaryotic ribosome biogenesis, the ribosomal proteins must be imported into the nucleus for assembly. In general, proteins which are capable of entering the nucleus usually contain a nuclear localization signal (NLS). In this study, we first used all available NLS prediction programs to search the presence of NLS in all eukaryotic ribosomal proteins, and found RPS4, RPS20, RPL10, RPL17, RPL18 and RPL31 do not contain any predicted NLS. To verify the nature of such ribosomal proteins, we used a flag-tagging approach to see whether these proteins are able to reach nucleus or not. The results show that FLAG-S4, FLAG-L17, and FLAG-L31 have made into the nucleus, whereas FLAG-S20 resides at cytoplasm; furthermore, of particularly interest is that FLAG-L10 and FLAG-L18 have been located at the plasma membrane. Accordingly, we have continued to investigate the nature of RPL10 with respect to it cellular distribution. The mutant FLAG-L10D183K carrying a deletion of a putative PDZ domain binding motif (PBM) at the C-terminal end allows the protein to be transported from the membrane to the nucleus, suggesting that the nuclear entry of RPL10 could be membrane-binding dependent. Interestingly, during examination of the cellular distribution of FLAG-L10, we also found that on rare occasions, FLAG-L10 can be located within the nucleus and nucleoli in dividing cells. This implies that the nuclear import of RPL10 could be cell cycle dependent. By transfecting a FLAG-L10 gene into synchronized cells, we have found that FLAG-L10 reaches the nucleus and nucleoli during the G1 phase. To understand the mechanism behind such an unusual phenomenon of nuclear uptake, we intend to use a GST-pull down assay to search for possible proteins that may facilitate the nuclear import or involve in the plasma membrane association of RPL10.
Ping-HanChung and 鍾秉翰. "Ribosomal protein L19 regulates CCND1 protein expression and cell cycle progression through interacting with the internal ribosome entry site located on the 5’UTR of CCND1 mRNA." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/75338023090296390942.
Повний текст джерела國立成功大學
生物資訊與訊息傳遞研究所
100
Ribosome is composed of rRNAs, ribosomal proteins, and many non-ribosomal factors to conduct the translation function. Traditionally, ribosomal proteins were considered as co-factors to execute the protein translation. But, numerous studies have demonstrated that ribosomal proteins not only play as co-factors of translational complex but also regulate the protein synthesis of specific mRNAs. RPL19 is a component of ribosome large subunit which belonged to the L-19E super-family and conserved among eukaryotes. In previous study, RPL19 was reported to have an impact on cyclin D1 protein expression but not on other cell cycle regulators, which indicated RPL19 may be a regulator of specific cell cycle regulators. During cell cycle progression, internal ribosome entry site (IRES) was reported to mediate the translational regulation of many cell cycle regulators. Since cyclin D1 expression was reported to be regulated by RPL19 and the 5’UTR of cyclin D1 mRNA carries a potential IRES element, the hypothesis was reported that RPL19 may regulate the expression of cyclin D1 through IRES. To address it, cells were synchronized and following experiments were conducted. First, western blot analysis showed that RPL19 expression level remained unchanged during cell cycle progression. However, RNA-IP showed that RPL19 interacted with cyclin D1 mRNAs at G1/S boundary. Bicistronic reporter assay showed that the 5’UTR of cyclin D1 had strong IRES activity and was regulated by RPL19. IRES-mediated translation regulation is often facilitated with the help of IRES trans-acting factors (ITAFs). RPL19 cooperated with a known ITAF, hnRNP A1, to regulate the IRES activity of cyclin D1. Furthermore, we observed that down-regulation of RPL19 significantly decreased the proliferation rate of HeLa cells. To sum up, we identified that RPL19, a ribosomal protein, can cooperate with hnRNPA1 to regulate cell cycle progression through regulating the IRES activity of cyclin D1.
Hamman, Brian D. "The conformational dynamics and subunit equilibrium of Escherichia coli ribosomal protein L7/L12." Thesis, 1994. http://hdl.handle.net/10125/9378.
Повний текст джерелаYu-ZhenWu and 吳榆蓁. "To identify the functional role of ribosomal protein L19 (RPL19) in the cancer development." Thesis, 2019. http://ndltd.ncl.edu.tw/handle/fcfc5j.
Повний текст джерелаWu, Jing-Yiing, and 吳京穎. "The Interaction between the Ribosomal Proteins and Endoplasmic Reticulum(ER):The role of large subunit ribosomal proteins L17 and L26 in making rough ER." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/01768869824988472328.
Повний текст джерела國立陽明大學
遺傳學研究所
92
The interaction between the ribosome and ER (endoplasmic reticulum) has been revealed by cryo-electron microscopy at 15.4Å resolution. The information predicts that four contact points, namely L19, L25, L26 and L35 of ribosome, provide the major attachments to the ER. So far, no direct biochemical evidence has been given in respect to the attachments. This thesis intends to investigate the binding of human ribosomal protein L17 and L26 to the ER. In this study I have demonstrated that the phosphorylation- tagged L17 and that of L26 can be assembled into recombinant ribosomes, and maintain a normal functions in translation. In addition I have detected that the using phosphorylation probing C-terminal regions of L17 and that of L26 expose on the surface of the ribosome. In test of purified ribosomal proteins binding the rough ER it shows that the L17 and L26 can bind to ER by the microsome floating assay. Furthermore, in a cross-linking experiment I have observed that L17 does not crosslink to the components of translocon protein complex, but rather associates with other high molecular weight proteins of ER. This result of this study has provided a useful information in understanding the mechanism of protein translocation.
Lu, Nan Chi, and 呂南畿. "Crystallization Studies of Rhizopus oryzae Aspartic Protease, Helicobacter pylori Ribosomal Protein L7/L12 and Corynebacterium glutamicum Citrate Synthase." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/36475413530930947866.
Повний текст джерела國立清華大學
分子與細胞生物研究所
93
Rhizopus oryzae aspartic protease is the endopeptidase that depends on aspartic acid residues for their catalytic activity. The intensity of the bitterness is proportional to the number of hydrophobic amino acids and basic amino acids in the hydrolysate. Rhizopus oryzae aspartic protease has a high specificity for hydrophobic amino acids and hence has a great potential for debittering. In this study, we aimed to determine the X-ray crystallographic structure of aspartic protease from Rhizopus oryzae. Crystals grew in the conditions using 25 % PEG MME 2000, 0.2 M ammonium sulfate, 0.1 M sodium-acetate (pH 4.2) as precipitant at 20 ℃. Crystals diffracted beyond a resolution of 1.1 Å and were found to belong to space group P41212, with unit-cell parameters of a=b=68.8 Å, c=132.2 Å, α=β=γ=900. Attempts to solve the phases with heavy-atom soaking using the multiple-wavelength anomalous diffraction (MAD) method were nonetheless failed. This structure was later solved by Jai-shin Liu with molecular replacement method. The other crystallization studies were focused on ribosomal protein L7/L12 of Helicobacter pylori (HP1199) and citrate synthase of Corynebacterium glutamicum. Needle-like crystals of HP1199 were obtained that lacked diffraction, while citrate synthase is still under crystallization trails.
Drygin, Denis. "Studies of the complex of ribosomal protein L1 with its binding site in 23S rRNA: Modification -interference, mutagenesis and crosslinking." 2002. https://scholarworks.umass.edu/dissertations/AAI3039352.
Повний текст джерела