Relevant bibliographies by topics / L11 Ribosomal Protein

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Academic literature on the topic 'L11 Ribosomal Protein'

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Published: 6 September 2023

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Journal articles on the topic "L11 Ribosomal Protein"

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Ramirez, Celia, Lawrence C. Shimmin, C. Hunter Newton, Alastair T. Matheson, and Patrick P. Dennis. "Structure and evolution of the L11, L1, L10, and L12 equivalent ribosomal proteins in eubacteria, archaebacteria, and eucaryotes." Canadian Journal of Microbiology 35, no. 1 (January 1, 1989): 234–44. http://dx.doi.org/10.1139/m89-036.

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The genes corresponding to the L11, L1, L10, and L12 equivalent ribosomal proteins (L11e, L1e, L10e, and L12e) of Escherichia coli have been cloned and sequenced from two widely divergent species of archaebacteria, Halobacterium cutirubrum and Sulfolobus solfataricus, and the L10 and four different L12 genes have been cloned and sequenced from the eucaryote Saccharomyces cerevisiae. Alignments between the deduced amino acid sequences of these proteins and to other available homologous proteins of eubacteria and eucaryotes have been made. The data suggest that the archaebacteria are a distinct coherent phylogenetic group. Alignment of the proline-rich L11e proteins reveals that the N-terminal region, believed to be responsible for interaction with release factor 1, is the most highly conserved region and that there is specific conservation of most of the proline residues, which may be important in maintaining the highly elongated structure of the molecule. Although L11 is the most highly methylated protein in the E. coli ribosome, the sites of methylation are not conserved in the archaebacterial L11e proteins. The L1e proteins of eubacteria and archaebacteria show two regions of very high similarity near the center and the carboxy termini of the proteins. The L10e proteins of all kingdoms are colinear and contain approximately three fourths of an L12e protein fused to their carboxy terminus, although much of this fusion has been lost in the truncated eubacterial protein. The archaebacterial and eucaryotic L12e proteins are colinear, whereas the eubacterial protein has suffered a rearrangement through what appear to be gene fusion events. Within the L12e derived region of the L10e proteins there exists a repeated module of 26 amino acids, present in two copies in eucaryotes, three in archaebacteria, and one in eubacteria. This modular sequence is apparently also present in the L12e proteins of all kingdoms and may play a role in L12e dimerization, L10e–L12e complex formation, and the function of the L10e–L12e complex in translation.Key words: translation, ribosome.
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Mitroshin, Ivan, Maria Garber, and Azat Gabdulkhakov. "Crystallographic analysis of archaeal ribosomal protein L11." Acta Crystallographica Section F Structural Biology Communications 71, no. 8 (July 29, 2015): 1083–87. http://dx.doi.org/10.1107/s2053230x15011395.

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Ribosomal protein L11 is an important part of the GTPase-associated centre in ribosomes of all organisms. L11 is a highly conserved two-domain ribosomal protein. The C-terminal domain of L11 is an RNA-binding domain that binds to a fragment of 23S rRNA and stabilizes its structure. The complex between L11 and 23S rRNA is involved in the GTPase activity of the translation elongation and release factors. Bacterial and archaeal L11–rRNA complexes are targets for peptide antibiotics of the thiazole class. To date, there is no complete structure of archaeal L11 owing to the mobility of the N-terminal domain of the protein. Here, the crystallization and X-ray analysis of the ribosomal protein L11 fromMethanococcus jannaschiiare reported. Crystals of the native protein and its selenomethionine derivative belonged to the orthorhombic space groupI222 and were suitable for structural studies. Native and single-wavelength anomalous dispersion data sets have been collected and determination of the structure is in progress.
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Yang, Xiaoming, and Edward E. Ishiguro. "Involvement of the N Terminus of Ribosomal Protein L11 in Regulation of the RelA Protein of Escherichia coli." Journal of Bacteriology 183, no. 22 (November 15, 2001): 6532–37. http://dx.doi.org/10.1128/jb.183.22.6532-6537.2001.

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ABSTRACT Amino acid-deprived rplK (previously known asrelC) mutants of Escherichia coli cannot activate (p)ppGpp synthetase I (RelA) and consequently exhibit relaxed phenotypes. The rplK gene encodes ribosomal protein L11, suggesting that L11 is involved in regulating the activity of RelA. To investigate the role of L11 in the stringent response, a derivative ofrplK encoding L11 lacking the N-terminal 36 amino acids (designated ′L11) was constructed. Bacteria overexpressing ′L11 exhibited a relaxed phenotype, and this was associated with an inhibition of RelA-dependent (p)ppGpp synthesis during amino acid deprivation. In contrast, bacteria overexpressing normal L11 exhibited a typical stringent response. The overexpressed ′L11 was incorporated into ribosomes and had no effect on the ribosome-binding activity of RelA. By several methods (yeast two-hybrid, affinity blotting, and copurification), no direct interaction was observed between the C-terminal ribosome-binding domain of RelA and L11. To determine whether the proline-rich helix of L11 was involved in RelA regulation, the Pro-22 residue was replaced with Leu by site-directed mutagenesis. The overexpression of the Leu-22 mutant derivative of L11 resulted in a relaxed phenotype. These results indicate that the proline-rich helix in the N terminus of L11 is involved in regulating the activity of RelA.
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Cameron, Dale M., Steven T. Gregory, Jill Thompson, Moo-Jin Suh, Patrick A. Limbach, and Albert E. Dahlberg. "Thermus thermophilus L11 Methyltransferase, PrmA, Is Dispensable for Growth and Preferentially Modifies Free Ribosomal Protein L11 Prior to Ribosome Assembly." Journal of Bacteriology 186, no. 17 (September 1, 2004): 5819–25. http://dx.doi.org/10.1128/jb.186.17.5819-5825.2004.

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ABSTRACT The ribosomal protein L11 in bacteria is posttranslationally trimethylated at multiple amino acid positions by the L11 methyltransferase PrmA, the product of the prmA gene. The role of L11 methylation in ribosome function or assembly has yet to be determined, although the deletion of Escherichia coli prmA has no apparent phenotype. We have constructed a mutant of the extreme thermophile Thermus thermophilus in which the prmA gene has been disrupted with the htk gene encoding a heat-stable kanamycin adenyltransferase. This mutant shows no growth defects, indicating that T. thermophilus PrmA, like its E. coli homolog, is dispensable. Ribosomes prepared from this mutant contain unmethylated L11, as determined by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), and are effective substrates for in vitro methylation by cloned and purified T. thermophilus PrmA. MALDI-TOF MS also revealed that T. thermophilus L11 contains a total of 12 methyl groups, in contrast to the 9 methyl groups found in E. coli L11. Finally, we found that, as with the E. coli methyltransferase, the ribosomal protein L11 dissociated from ribosomes is a more efficient substrate for in vitro methylation by PrmA than intact 70S ribosomes, suggesting that methylation in vivo occurs on free L11 prior to its incorporation into ribosomes.
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Bailly, Christian, and Gérard Vergoten. "Interaction of Camptothecin Anticancer Drugs with Ribosomal Proteins L15 and L11: A Molecular Docking Study." Molecules 28, no. 4 (February 15, 2023): 1828. http://dx.doi.org/10.3390/molecules28041828.

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The antitumor drug topotecan (TPT) is a potent inhibitor of topoisomerase I, triggering DNA breaks lethal for proliferating cancer cells. The mechanism is common to camptothecins SN38 (the active metabolite of irinotecan) and belotecan (BLT). Recently, TPT was shown to bind the ribosomal protein L15, inducing an antitumor immune activation independent of topoisomerase I. We have modeled the interaction of four camptothecins with RPL15 derived from the 80S human ribosome. Two potential drug-binding sites were identified at Ile135 and Phe129. SN38 can form robust RPL15 complexes at both sites, whereas BLT essentially gave stable complexes with site Ile135. The empirical energy of interaction (ΔE) for SN38 binding to RPL15 is similar to that determined for TPT binding to the topoisomerase I-DNA complex. Molecular models with the ribosomal protein L11 sensitive to topoisomerase inhibitors show that SN38 can form a robust complex at a single site (Cys25), much more stable than those with TPT and BLT. The main camptothecin structural elements implicated in the ribosomal protein interaction are the lactone moiety, the aromatic system and the 10-hydroxyl group. The study provides guidance to the design of modulators of ribosomal proteins L11 and L15, both considered anticancer targets.
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Remacha, Miguel, Antonio Jimenez-Diaz, Cruz Santos, Elisa Briones, Reina Zambrano, M. A. Rodriguez Gabriel, E. Guarinos, and Juan P. G. Ballesta. "Proteins P1, P2, and P0, components of the eukaryotic ribosome stalk. New structural and functional aspects." Biochemistry and Cell Biology 73, no. 11-12 (December 1, 1995): 959–68. http://dx.doi.org/10.1139/o95-103.

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The eukaryoic ribosomal stalk is thought to consist of the phosphoproteins P1 and P2, which form a complex with protein P0. This complex interacts at the GTPase domain in the large subunit rRNA, overlapping the binding site of the protein L11-like eukaryotic counterpart (Saccharomyces cerevisiae protein L15 and mammalian protein LI2). An unusual pool of the dephosphorylated forms of proteins P1 and P2 is detected in eukaryotic cytoplasm, and an exchange between the proteins in the pool and on the ribosome takes place during translation. Quadruply disrupted yeast strains, carrying four inactive acidic protein genes and, therefore, containing ribosomes totally depleted of acidic proteins, are viable but grow with a doubling time threefold higher than wild-type cells. The in vitro translation systems derived from these stains are active but the two-dimensional gel electrophoresis pattern of proteins expressed in vivo and in vitro is partially different. These results indicate that the P1 and P2 proteins are not essential for ribosome activity but are able to affect the translation of some specific mRNAs. Protein P0 is analogous to bacterial ribosomal protein L10 but carries an additional carboxyl domain showing a high sequence homology to the acidic proteins P1 and P2, including the terminal peptide DDDMGFGLFD. Successive deletions of the P0 carboxyl domain show that removal of the last 21 amino acids from the P0 carboxyl domain only slightly affects the ribosome activity in a wild-type genetic background; however, the same deletion is lethal in a quadruple disruptant deprived of acidic P1/P2 proteins. Additional deletions affect the interaction of P0 with the P1 and P2 proteins and with the rRNA. The experimental data available support the implication of the eukaryotic stalk components in some regulatory process that modulates the ribosomal activity.Key words: ribosomal stalk, acidic proteins, phosphorylation, GTPase domain, translation regulation.
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Kraft, Alexander, Christina Lutz, Arno Lingenhel, Peter Gröbner, and Wolfgang Piendl. "Control of Ribosomal Protein L1 Synthesis in Mesophilic and Thermophilic Archaea." Genetics 152, no. 4 (August 1, 1999): 1363–72. http://dx.doi.org/10.1093/genetics/152.4.1363.

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Abstract The mechanisms for the control of ribosomal protein synthesis have been characterized in detail in Eukarya and in Bacteria. In Archaea, only the regulation of the MvaL1 operon (encoding ribosomal proteins MvaL1, MvaL10, and MvaL12) of the mesophilic Methanococcus vannielii has been extensively investigated. As in Bacteria, regulation takes place at the level of translation. The regulator protein MvaL1 binds preferentially to its binding site on the 23S rRNA, and, when in excess, binds to the regulatory target site on its mRNA and thus inhibits translation of all three cistrons of the operon. The regulatory binding site on the mRNA, a structural mimic of the respective binding site on the 23S rRNA, is located within the structural gene about 30 nucleotides downstream of the ATG start codon. MvaL1 blocks a step before or at the formation of the first peptide bond of MvaL1. Here we demonstrate that a similar regulatory mechanism exists in the thermophilic M. thermolithotrophicus and M. jannaschii. The L1 gene is cotranscribed together with the L10 and L11 gene, in all genera of the Euryarchaeota branch of the Archaea studied so far. A potential regulatory L1 binding site located within the structural gene, as in Methanococcus, was found in Methanobacterium thermoautotrophicum and in Pyrococcus horikoshii. In contrast, in Archaeoglobus fulgidus a typical L1 binding site is located in the untranslated leader of the L1 gene as described for the halophilic Archaea. In Sulfolobus, a member of the Crenarchaeota, the L1 gene is part of a long transcript (encoding SecE, NusG, L11, L1, L10, L12). A previously suggested regulatory L1 target site located within the L11 structural gene could not be confirmed as an L1 binding site.
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Liao, Daiqing, and Patrick P. Dennis. "Molecular phylogenies based on ribosomal protein L11, L1, L10, and L12 sequences." Journal of Molecular Evolution 38, no. 4 (April 1994): 405–19. http://dx.doi.org/10.1007/bf00163157.

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Zhang, Yanping, Gabrielle White Wolf, Krishna Bhat, Aiwen Jin, Theresa Allio, William A. Burkhart, and Yue Xiong. "Ribosomal Protein L11 Negatively Regulates Oncoprotein MDM2 and Mediates a p53-Dependent Ribosomal-Stress Checkpoint Pathway." Molecular and Cellular Biology 23, no. 23 (December 1, 2003): 8902–12. http://dx.doi.org/10.1128/mcb.23.23.8902-8912.2003.

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ABSTRACT The gene encoding p53 mediates a major tumor suppression pathway that is frequently altered in human cancers. p53 function is kept at a low level during normal cell growth and is activated in response to various cellular stresses. The MDM2 oncoprotein plays a key role in negatively regulating p53 activity by either direct repression of p53 transactivation activity in the nucleus or promotion of p53 degradation in the cytoplasm. DNA damage and oncogenic insults, the two best-characterized p53-dependent checkpoint pathways, both activate p53 through inhibition of MDM2. Here we report that the human homologue of MDM2, HDM2, binds to ribosomal protein L11. L11 binds a central region in HDM2 that is distinct from the ARF binding site. We show that the functional consequence of L11-HDM2 association, like that with ARF, results in the prevention of HDM2-mediated p53 ubiquitination and degradation, subsequently restoring p53-mediated transactivation, accumulating p21 protein levels, and inducing a p53-dependent cell cycle arrest by canceling the inhibitory function of HDM2. Interference with ribosomal biogenesis by a low concentration of actinomycin D is associated with an increased L11-HDM2 interaction and subsequent p53 stabilization. We suggest that L11 functions as a negative regulator of HDM2 and that there might exist in vivo an L11-HDM2-p53 pathway for monitoring ribosomal integrity.
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Zhang, Shuyu, Janelle M. Scott, and W. G. Haldenwang. "Loss of Ribosomal Protein L11 Blocks Stress Activation of the Bacillus subtilis Transcription Factor ςB." Journal of Bacteriology 183, no. 7 (April 1, 2001): 2316–21. http://dx.doi.org/10.1128/jb.183.7.2316-2321.2001.

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ABSTRACT ςB, the general stress response sigma factor ofBacillus subtilis, is activated when the cell's energy levels decline or the bacterium is exposed to environmental stress (e.g., heat shock, ethanol). Physical stress activates ςBthrough a collection of regulatory kinases and phosphatases (the Rsb proteins) which catalyze the release of ςB from an anti-ςB factor inhibitor. The means by which diverse stresses communicate with the Rsb proteins is unknown; however, a role for the ribosome in this process was suggested when several of the upstream members of the ςB stress activation cascade (RsbR, -S, and -T) were found to cofractionate with ribosomes in crudeB. subtilis extracts. We now present evidence for the involvement of a ribosome-mediated process in the stress activation of ςB. B. subtilis strains resistant to the antibiotic thiostrepton, due to the loss of ribosomal protein L11 (RplK), were found to be blocked in the stress activation of ςB. Neither the energy-responsive activation of ςB nor stress-dependent chaperone gene induction (a ςB-independent stress response) was inhibited by the loss of L11. The Rsb proteins required for stress activation of ςB are shown to be active in the RplK−strain but fail to be triggered by stress. The data demonstrate that the B. subtilis ribosomes provide an essential input for the stress activation of ςB and suggest that the ribosomes may themselves be the sensors for stress in this system.
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Dissertations / Theses on the topic "L11 Ribosomal Protein"

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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.

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Bouakaz, 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.

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Gilkes, 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.

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Petrov, 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.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2006.
Thesis 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.
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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.

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Ribosomal stalk proteins are known to play important role in protein synthesis. The ‘stalk’, an extended structure on the large subunit of the ribosome is composed mainly of two to three dimers of L12 and one L10 protein, which forms the base of the stalk. In E. coli, four copies of L12 molecules exist as dimer of dimers forming the pentameric L8 complex together with L10. This thesis is a collection of four interlinked studies on the structure, function and application of the ribosomal stalk protein L12. In the first study, we have mapped the interaction sites of the four major translation GTPase factors (IF2, EF-Tu, EF-G & RF3) on L12 molecule using heteronuclear NMR spectroscopy. Surprisingly, all these factors produced an overlapping interaction map spanning two α-helices on the C terminal domain of L12, thereby suggesting a general nature of the interaction between L12 and the GTPase factors. L12 is known to stimulate GTPase activity of the elongation factors EF-Tu and EF-G. Here, we have clarified the role of L12 in IF2 mediated initiation of protein synthesis. Our data suggest that rapid subunit association requires a specific interaction between the L12 protein on the 50S and IF2·GTP on the 30S preinitiation complex. We have also shown that L12 is not a GAP for IF2 and GTP hydrolysis triggers IF2 release from the 70S initiation complex. The next question we have addressed is why multiple copies of L12 dimer are needed on the ribosome. For this purpose, we created a pure E. coli strain JE105, where the terminal part of rplJ gene coding for the binding site of one L12 dimer on protein L10 was deleted in the chromosomal locus. Using ribosomes with single L12 dimer we have observed that the rate of the initiation and elongation involving IF2 and EF-G gets most compromised, which in turn decreases the growth rate of the bacteria.  This study also indicates that L12 can interact with different GTPase factors in a specialized manner. Lastly, we have developed an application making advantage of the multiple L12 dimers on the ribosome. By inserting a (His)6-tag at the C-terminus of the L12 protein we have created a novel E. coli strain (JE28), where all ribosomes are tetra-(His)6-tagged. Further, we have developed a single step method for purification of the active (His)6-tagged ribosomes from JE28.
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Simmons, 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.

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Thesis (M.S.) -- University of Maryland, College Park, 2005.
Thesis 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.
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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/.

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A proteína ribossomal L10 (RP L10) é uma forte candidata a ser incluída na classe de proteínas supressoras de tumor. Também denominada QM, a proteína em questão é conhecida por participar da ligação das subunidades ribossomais 60S e 40S e da tradução de mRNAs. Possui massa molecular entre 24 a 26 kDa e ponto isoelétrico (pI) 10,5. A seqüência da proteína QM é bastante conservada em mamíferos, plantas, invertebrados, insetos e leveduras indicando que esta possui funções críticas na célula. Com função supressora de tumor, a proteína RP L10 foi estudada em linhagens de tumor de Wilm (WT-1) e em células tumorais de estômago, nas quais se observou uma diminuição na quantidade de seu mRNA. Mais recentemente a RP L10 foi encontrada em baixas quantidades nos estágios iniciais de adenoma de próstata e com uma mutação em câncer de ovário, indicando uma participação no desenvolvimento destas doenças. Como proteína, já foi descrito que esta interage com as proteínas c-Jun e c-Yes, inibindo a ação ativadora de fatores de crescimento e divisão celular. Este trabalho tem um papel importante no estabelecimento da expressão desta proteína solúvel, para estudos posteriores que tenham como objetivo avaliar a ação de regiões específicas que atuam na ligação das subunidades ribossomais 60S e 40S e tradução, bem como nas regiões que se ligam a proto-oncogenes. O cDNA para proteína QM foi amplificado por PCR e clonado no vetor de expressão periplásmica p3SN8. A proteína QM foi expressa em E.coli BL21 (DE3) no citoplasma e periplasma bacteriano e na melhor condição, a expressão de QM de bactérias transformadas pelo plasmídeo recombinante p1813_QM em 25°C ou 30°C, a proteína foi obtida solúvel e com quantidad es muito pequenas de contaminantes. Os ensaios de estrutura secundária demonstraram que a proteína QM tem predominância de a-hélice, mas quando do seu desenovelmento, essa condição muda e a proteína passa a ter característica de folhas β.
The 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.
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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.

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Simoff, 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.

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Protein synthesis is a highly regulated and energy consuming process, during which a large ribonucleoprotein particle called the ribosome, synthesizes new proteins. The eukaryotic ribosome consists of two unequal subunits called: small and large subunits. Both subunits are composed of ribosomal RNA (rRNA) and ribosomal proteins (r-proteins). Although rRNAs build the matrix of the ribosome and carries out catalysing of the peptide-bond formation between amino acids, r-proteins also appear to play important structural and functional roles. The primary role of r-proteins is to initiate the correct tertiary fold of rRNA and to organize the overall structure of the ribosome. In this thesis, I focus on two proteins from the large subunit of the eukaryotic ribosome: r-proteins L5 and L15 from bakers yeast S. cerevisiae. Both r-proteins are essential for ribosome function. Their life cycle is primarily associated with rRNA interactions. As a consequence, the proteins show high sequence homology across the species borders. Furthermore, both L5 and L15 are connected to human diseases, which makes the study their role in ribosome biogenesis and ribosome function important. By applying random- and site-directed mutagenesis, coupled with functional complementation tests, I aimed to elucidate functionally regions in both proteins, implicated in transport to the cell nucleus, protein-protein interactions and/or rRNA binding. The importance of individual and multiple amino acid exchanges in the primary sequence of rpL5 and rpL15 were studied in vivo. The obtained results show that S. cerevisiae rpL15 was tolerant to amino acid exchanges in the primary sequence, whereas rpL5 was not. Consequently, A. thaliana rpL15 could substitute for the function of wild type rpL15, whereas none of the tested orthologous proteins to rpL5 could substitute yeast rpL5 in vivo. These observations further emphasize the importance of studying r-proteins as separate entities in the ribosome context.
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Fu, Yang. "Identification and Characterization of Novel Ribosomal Protein-binding RNA motifs in Bacteria." Thesis, Boston College, 2014. http://hdl.handle.net/2345/3795.

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Thesis advisor: Michelle M. Meyer
As 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
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Books on the topic "L11 Ribosomal Protein"

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Climie, Shane Christopher. mRNA secondary structure and feedback regulation of the L10 ribosomal protein operon of "Escherichia coli". 1988.

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Book chapters on the topic "L11 Ribosomal Protein"

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Draper, David E., Graeme L. Conn, Apostolos G. Gittis, Debraj Guhathakurta, Eaton E. Lattman, and Luis Reynaldo. "RNA Tertiary Structure and Protein Recognition in an L11-RNA Complex." In The Ribosome, 105–14. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818142.ch11.

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Schmidt, Jürgen, Wolfgang Weglöhner, and Alap R. Subramanian. "The Nuclear Genes for Chloroplast Ribosomal Proteins L11 and L12 in Higher Plants." In The Translational Apparatus, 555–64. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2407-6_52.

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Traut, R. R., D. S. Tewari, A. Sommer, G. R. Gavino, H. M. Olson, and D. G. Glitz. "Protein Topography of Ribosomal Functional Domains: Effects of Monoclonal Antibodies to Different Epitopes in Escherichia coli Protein L7/L12 on Ribosome Function and Structure." In Springer Series in Molecular Biology, 286–308. New York, NY: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4612-4884-2_17.

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Wu, Qi, Xiuzhen Wang, Hongtao Yu, Yufei Ding, Fenggao Cui, Jiancheng Zhang, Yueyi Tang, and Chuantang Wang. "Molecular Characterization and Expression of Ribosomal Protein L15 Gene (RPL15) From Arachis hypogaea." In Proceedings of the 2012 International Conference on Applied Biotechnology (ICAB 2012), 1171–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-37922-2_125.

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Traut, Robert R., Andrew V. Oleinikov, Evgeny Makarov, George Jokhadze, Bertrand Perroud, and Bruce Wang. "Structure and Function of Escherichia Coli Ribosomal Protein L7/L12: Effect of Cross-Links and Deletions." In The Translational Apparatus, 521–32. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2407-6_49.

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Fragapane, Paola, Elisa Caffarelli, Paola Mazzetti, Matteo Lener, Paola Pierandrei-Amaldi, and Irene Bozzoni. "Splicing Control and Nucleus/Cytoplasm Compartmentalization of Ribosomal Protein L1 RNA in X. Laevis Oocytes." In Nuclear Structure and Function, 95–98. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0667-2_19.

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Takaku, Hiroaki, Masamichi Takagi, and Akinori Ohta. "Isolation of a GCN4 Gene Analog and Determination of Its Involvement in Induction of Cycloheximide-Resistant Ribosomal Protein L41-Q in Candida maltosa." In Non-Conventional Yeasts in Genetics, Biochemistry and Biotechnology, 29–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55758-3_5.

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Conference papers on the topic "L11 Ribosomal Protein"

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Sun, Xiao-Xin, and Mushui Dai. "Abstract 1104: Perturbation of 60S ribosomal biogenesis results in ribosomal protein L5 and L11-dependent p53 activation." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1104.

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Li, Jun, Yiling Hou, Maojie Tian, Shibin Yuan, Bing Sun, Xiulan Su, Guangfu Wu, Yan Song, and Wanru Hou. "Cloning and sequence analysis of ribosomal protein L11 gene (rpL11) from the Ailuropoda melanoleuca." In 2010 3rd International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2010. http://dx.doi.org/10.1109/bmei.2010.5639420.

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Yang Hu, Jun Yang, Yi-Ling Hou, Xiang Ding, Zheng-Song Peng, and Wan-Ru Hou. "Cloning and sequence analysis of ribosomal protein L18 gene (rpl18) from Ailuropoda melanoleuca." In 2012 International Conference on Computer Science and Information Processing (CSIP). IEEE, 2012. http://dx.doi.org/10.1109/csip.2012.6308909.

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Si-Nan Zhang, Wan-Ru Hou, Jun Yang, Xiang Ding, Yi-Ling Hou, and Zheng-Song Peng. "Cloning and sequence analysis of ribosomal protein L13 gene (rpL13) from Ailuropoda melanoleuca." In 2012 International Conference on Computer Science and Information Processing (CSIP). IEEE, 2012. http://dx.doi.org/10.1109/csip.2012.6308911.

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Sun Jing-Hui, Wan-Ru Hou, Wu Chun-Lian, Yi-Ling Hou, and Ding Xiang. "cDNA, genomic sequence cloning, analyzing of ribosomal protein L19 from Ailuropoda melanoleuca and its overexpression." In 2012 International Conference on Computer Science and Information Processing (CSIP). IEEE, 2012. http://dx.doi.org/10.1109/csip.2012.6308904.

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Xiang-Hui Li, Yi-Ling Hou, Xiang Ding, Wan-Ru Hou, Jun Yang, and Zheng-Song Peng. "CDNA, genomic sequence cloning and sequence analysis of ribosomal protein L14 gene(rpL14) from Ailuropoda melanoleuca." In 2012 International Conference on Computer Science and Information Processing (CSIP). IEEE, 2012. http://dx.doi.org/10.1109/csip.2012.6308910.

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Reports on the topic "L11 Ribosomal Protein"

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Bercovier, Herve, Raul Barletta, and Shlomo Sela. Characterization and Immunogenicity of Mycobacterium paratuberculosis Secreted and Cellular Proteins. United States Department of Agriculture, January 1996. http://dx.doi.org/10.32747/1996.7573078.bard.

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Our long-term goal is to develop an efficient acellular vaccine against paratuberculosis based on protein antigen(s). A prerequisite to achieve this goal is to analyze and characterize Mycobacterium paratuberculosis (Mpt) secreted and cellular proteins eliciting a protective immune response. In the context of this general objective, we proposed to identify, clone, produce, and characterize: the Mpt 85B antigen and other Mpt immunoreactive secreted proteins, the Mpt L7/L12 ribosomal protein and other immunoreactive cellular proteins, Mpt protein determinants involved in invasion of epithelial cells, and Mpt protein antigens specifically expressed in macrophages. Paratuberculosis is still a very serious problem in Israel and in the USA. In the USA, a recent survey evaluated that 21.6% of the dairy herd were infected with Mpt resulting in 200-250 million dollars in annual losses. Very little is known on the virulence factors and on protective antigens of Mpt. At present, the only means of controlling this disease are culling or vaccination. The current vaccines do not allow a clear differentiation between infected and vaccinated animals. Our long-term goal is to develop an efficient acellular paratuberculosis vaccine based on Mpt protein antigen(s) compatible with diagnostic tests. To achieve this goal it is necessary to analyze and characterize secreted and cellular proteins candidate for such a vaccine. Representative Mpt libraries (shuttle plasmid and phage) were constructed and used to study Mpt genes and gene products described below and will be made available to other research groups. In addition, two approaches were performed which did not yield the expected results. Mav or Mpt DNA genes that confer upon Msg or E. coli the ability to invade and/or survive within HEp-2 cells were not identified. Likewise, we were unable to characterize the 34-39 kDa induced secreted proteins induced by stress factors due to technical difficulties inherent to the complexity of the media needed to support substantial M. pt growth. We identified, isolated, sequenced five Mpt proteins and expressed four of them as recombinant proteins that allowed the study of their immunological properties in sensitized mice. The AphC protein, found to be up regulated by low iron environment, and the SOD protein are both involved in protecting mycobacteria against damage and killing by reactive oxygen (Sod) and nitrogen (AhpC) intermediates, the main bactericidal mechanisms of phagocytic cells. SOD and L7/L12 ribosomal proteins are structural proteins constitutively expressed. 85B and CFP20 are both secreted proteins. SOD, L7/L12, 85B and CFP20 were shown to induce a Th1 response in immunized mice whereas AphC was shown by others to have a similar activity. These proteins did not interfere with the DTH reaction of naturally infected cows. Cellular immunity provides protection in mycobacterial infections, therefore molecules inducing cellular immunity and preferentially a Th1 pathway will be the best candidate for the development of an acellular vaccine. The proteins characterized in this grant that induce a cell-mediated immunity and seem compatible with diagnostic tests, are good candidates for the construction of a future acellular vaccine.
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Banai, Menachem, and Gary Splitter. Molecular Characterization and Function of Brucella Immunodominant Proteins. United States Department of Agriculture, July 1993. http://dx.doi.org/10.32747/1993.7568100.bard.

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The BARD project was a continuation of a previous BARD funded research project. It was aimed at characterization of the 12kDa immunodominant protein and subsequently the cloning and expression of the gene in E. coli. Additional immunodominant proteins were sought among genomic B. abortus expression library clones using T-lymphocyte proliferation assay as a screening method. The 12kDa protein was identified as the L7/L12 ribosomal protein demonstrating in the first time the role a structural protein may play in the development of the host's immunity against the organism. The gene was cloned from B. abortus (USA) and B. melitensis (Israel) showing identity of the oligonucleotide sequence between the two species. Further subcloning allowed expression of the protein in E. coli. While the native protein was shown to have DTH antigenicity its recombinant analog lacked this activity. In contrast the two proteins elicited lymphocyte proliferation in experimental murine brucellosis. CD4+ cells of the Th1 subset predominantly responded to this protein demonstrating the development of protective immunity (g-IFN, and IL-2) in the host. Similar results were obtained with bovine Brucella primed lymphocytes. UvrA, GroE1 and GroEs were additional Brucella immunodominant proteins that demonstrated MHC class II antigenicity. The role cytotoxic cells are playing in the clearance of brucella cells was shown using knock out mice defective either in their CD4+ or CD8+ cells. CD4+ defective mice were able to clear brucella as fast as did normal mice. In contrast mice which were defective in their CD8+ cells could not clear the organisms effectively proving the importance of this subtype cell line in development of protective immunity. The understanding of the host's immune response and the expansion of the panel of Brucella immunodominant proteins opened new avenues in vaccine design. It is now feasible to selectively use immunodominant proteins either as subunit vaccine to fortify immunity of older animals or as diagnostic reagents for the serological survaillance.
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