Relevant bibliographies by topics / RRNA Methyltransferase

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Academic literature on the topic 'RRNA Methyltransferase'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "RRNA Methyltransferase"

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Corrêa, Laís L., Marta A. Witek, Natalia Zelinskaya, Renata C. Picão, and Graeme L. Conn. "Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG." Antimicrobial Agents and Chemotherapy 60, no. 1 (2015): 699–702. http://dx.doi.org/10.1128/aac.02482-15.

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ABSTRACTThe exogenously acquired 16S rRNA methyltransferases RmtD, RmtD2, and RmtG were cloned and heterologously expressed inEscherichia coli, and the recombinant proteins were purified to near homogeneity. Each methyltransferase conferred an aminoglycoside resistance profile consistent with m7G1405 modification, and this activity was confirmed byinvitro30S methylation assays. Analyses of protein structure and interaction withS-adenosyl-l-methionine suggest that the molecular mechanisms of substrate recognition and catalysis are conserved across the 16S rRNA (m7G1405) methyltransferase family
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Savic, Miloje, S. Sunita, Natalia Zelinskaya, et al. "30S Subunit-Dependent Activation of the Sorangium cellulosum So ce56 Aminoglycoside Resistance-Conferring 16S rRNA Methyltransferase Kmr." Antimicrobial Agents and Chemotherapy 59, no. 5 (2015): 2807–16. http://dx.doi.org/10.1128/aac.00056-15.

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ABSTRACTMethylation of bacterial 16S rRNA within the ribosomal decoding center confers exceptionally high resistance to aminoglycoside antibiotics. This resistance mechanism is exploited by aminoglycoside producers for self-protection while functionally equivalent methyltransferases have been acquired by human and animal pathogenic bacteria. Here, we report structural and functional analyses of theSorangium cellulosumSo ce56 aminoglycoside resistance-conferring methyltransferase Kmr. Our results demonstrate that Kmr is a 16S rRNA methyltransferase acting at residue A1408 to confer a canonical
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Nosrati, Meisam, Debayan Dey, Atousa Mehrani, et al. "Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition." Journal of Biological Chemistry 294, no. 46 (2019): 17642–53. http://dx.doi.org/10.1074/jbc.ra119.011181.

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Methylation of the small ribosome subunit rRNA in the ribosomal decoding center results in exceptionally high-level aminoglycoside resistance in bacteria. Enzymes that methylate 16S rRNA on N7 of nucleotide G1405 (m7G1405) have been identified in both aminoglycoside-producing and clinically drug-resistant pathogenic bacteria. Using a fluorescence polarization 30S-binding assay and a new crystal structure of the methyltransferase RmtC at 3.14 Å resolution, here we report a structure-guided functional study of 30S substrate recognition by the aminoglycoside resistance-associated 16S rRNA (m7G140
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Chen, Hao, Zhennan Shi, Jiaojiao Guo, et al. "The human mitochondrial 12S rRNA m4C methyltransferase METTL15 is required for mitochondrial function." Journal of Biological Chemistry 295, no. 25 (2020): 8505–13. http://dx.doi.org/10.1074/jbc.ra119.012127.

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Mitochondrial DNA gene expression is coordinately regulated both pre- and post-transcriptionally, and its perturbation can lead to human pathologies. Mitochondrial rRNAs (mt-rRNAs) undergo a series of nucleotide modifications after release from polycistronic mitochondrial RNA precursors, which is essential for mitochondrial ribosomal biogenesis. Cytosine N4-methylation (m4C) at position 839 (m4C839) of the 12S small subunit mt-rRNA was identified decades ago; however, its biogenesis and function have not been elucidated in detail. Here, using several approaches, including immunofluorescence, R
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Rowe, Sebastian J., Ryan J. Mecaskey, Mohamed Nasef, et al. "Shared requirements for key residues in the antibiotic resistance enzymes ErmC and ErmE suggest a common mode of RNA recognition." Journal of Biological Chemistry 295, no. 51 (2020): 17476–85. http://dx.doi.org/10.1074/jbc.ra120.014280.

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Erythromycin-resistance methyltransferases are SAM dependent Rossmann fold methyltransferases that convert A2058 of 23S rRNA to m62A2058. This modification sterically blocks binding of several classes of antibiotics to 23S rRNA, resulting in a multidrug-resistant phenotype in bacteria expressing the enzyme. ErmC is an erythromycin resistance methyltransferase found in many Gram-positive pathogens, whereas ErmE is found in the soil bacterium that biosynthesizes erythromycin. Whether ErmC and ErmE, which possess only 24% sequence identity, use similar structural elements for rRNA substrate recog
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McGann, Patrick, Sarah Chahine, Darius Okafor, et al. "Detecting 16S rRNA Methyltransferases in Enterobacteriaceae by Use of Arbekacin." Journal of Clinical Microbiology 54, no. 1 (2015): 208–11. http://dx.doi.org/10.1128/jcm.02642-15.

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16S rRNA methyltransferases confer resistance to most aminoglycosides, but discriminating their activity from that of aminoglycoside-modifying enzymes (AMEs) is challenging using phenotypic methods. We demonstrate that arbekacin, an aminoglycoside refractory to most AMEs, can rapidly detect 16S methyltransferase activity inEnterobacteriaceaewith high specificity using the standard disk susceptibility test.
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White, Joshua, Zhihua Li, Richa Sardana, Janusz M. Bujnicki, Edward M. Marcotte, and Arlen W. Johnson. "Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits." Molecular and Cellular Biology 28, no. 10 (2008): 3151–61. http://dx.doi.org/10.1128/mcb.01674-07.

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ABSTRACT BUD23 was identified from a bioinformatics analysis of Saccharomyces cerevisiae genes involved in ribosome biogenesis. Deletion of BUD23 leads to severely impaired growth, reduced levels of the small (40S) ribosomal subunit, and a block in processing 20S rRNA to 18S rRNA, a late step in 40S maturation. Bud23 belongs to the S-adenosylmethionine-dependent Rossmann-fold methyltransferase superfamily and is related to small-molecule methyltransferases. Nevertheless, we considered that Bud23 methylates rRNA. Methylation of G1575 is the only mapped modification for which the methylase has n
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van Tran, Nhan, Felix G. M. Ernst, Ben R. Hawley, et al. "The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112." Nucleic Acids Research 47, no. 15 (2019): 7719–33. http://dx.doi.org/10.1093/nar/gkz619.

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Abstract N6-methyladenosine (m6A) has recently been found abundantly on messenger RNA and shown to regulate most steps of mRNA metabolism. Several important m6A methyltransferases have been described functionally and structurally, but the enzymes responsible for installing one m6A residue on each subunit of human ribosomes at functionally important sites have eluded identification for over 30 years. Here, we identify METTL5 as the enzyme responsible for 18S rRNA m6A modification and confirm ZCCHC4 as the 28S rRNA modification enzyme. We show that METTL5 must form a heterodimeric complex with T
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Ruszkowska, Agnieszka. "METTL16, Methyltransferase-Like Protein 16: Current Insights into Structure and Function." International Journal of Molecular Sciences 22, no. 4 (2021): 2176. http://dx.doi.org/10.3390/ijms22042176.

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Methyltransferase-like protein 16 (METTL16) is a human RNA methyltransferase that installs m6A marks on U6 small nuclear RNA (U6 snRNA) and S-adenosylmethionine (SAM) synthetase pre-mRNA. METTL16 also controls a significant portion of m6A epitranscriptome by regulating SAM homeostasis. Multiple molecular structures of the N-terminal methyltransferase domain of METTL16, including apo forms and complexes with S-adenosylhomocysteine (SAH) or RNA, provided the structural basis of METTL16 interaction with the coenzyme and substrates, as well as indicated autoinhibitory mechanism of the enzyme activ
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L. Aishwarya, K. V., P. V. Geetha, M. Shanthi, and S. Uma. "Co occurrence of two 16S rRNA methyltrasferases along with NDM and OXA 48 like carbapenamases on a single plasmid in Klebsiella pneumoniae." Journal of Laboratory Physicians 11, no. 04 (2019): 305–11. http://dx.doi.org/10.4103/jlp.jlp_59_19.

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Abstract BACKGROUND: The carbapenemase-encoding genes, bla NDM- and bla OXA-48 - like , confer resistance to all the known beta-lactams and are encountered along with other beta-lactamase-encoding genes and/or 16S ribosomal RNA (rRNA)-methylating genes. The co-occurrence of bla NDM and bla OXA-48 - like on a single plasmid is a rare occurrence. AIM AND OBJECTIVE: The purpose of the study was to characterize the plasmids in Klebsiella pneumoniae isolates producing 16S rRNA methyltransferase along with bla NDM , bla OXA-48-like , and other resistance encoding genes. MATERIALS AND METHODS: One-hu
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Dissertations / Theses on the topic "RRNA Methyltransferase"

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Zarubica, Tamara. "SPECIFICITY DETERMINANTS OF ArmA, A RIBOSOMAL RNA METHYLTRANSFERASE THAT CONFERS ANTIBIOTIC RESISTANCE." VCU Scholars Compass, 2010. http://scholarscompass.vcu.edu/etd/2273.

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Bacterial resistance to 4,6-type aminoglycoside antibiotics, which target the 30S ribosomal subunit, has been traced to the arm/rmt family of rRNA methyltransferases. These plasmid-encoded enzymes transfer a methyl group from S-adenosylmethionine to N7 of the buried G1405 in the aminoglycoside binding site of 16S rRNA in the 30S ribosomal subunit. Neither 16S rRNA alone nor intact 70S ribosome is an efficient substrate for armA methyltransferase. To more fully characterize this family of enzymes, xiii we have investigated the substrate requirements of ArmA. We determined the Mg2+ dependence of
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Kshetri, Man B. "N-TERMINAL DOMAIN OF rRNA METHYLTRANSFERASE ENZYME RsmC IS IMPORTANT FOR ITS BINDING TO RNA AND RNA CHAPERON ACTIVITY." Kent State University Honors College / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=ksuhonors1621007414429417.

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Treede, Irina. "Aufklärung der Funktion von zwei rRNA-Methyltransferasen und Untersuchungen zur Eurekanat-Biosynthese in Streptomyces viridochromogenes Tü57." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973266686.

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Punekar, Avinash S. "Ribosomal RNA Modification Enzymes : Structural and functional studies of two methyltransferases for 23S rRNA modification in Escherichia coli." Doctoral thesis, Uppsala universitet, Struktur- och molekylärbiologi, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-212394.

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Escherichia coli ribosomal RNA (rRNA) is post-transcriptionally modified by site-specific enzymes. The role of most modifications is not known and little is known about how these enzymes recognize their target substrates. In this thesis, we have structurally and functionally characterized two S-adenosyl-methionine (SAM) dependent 23S rRNA methyltransferases (MTases) that act during the early stages of ribosome assembly in E. coli. RlmM methylates the 2'O-ribose of C2498 in 23S rRNA. We have solved crystal structures of apo RlmM at 1.9Å resolution and of an RlmM-SAM complex at 2.6Å resolution.
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Sharma, Sunny [Verfasser], Karl-Dieter [Akademischer Betreuer] Entain, Jens [Akademischer Betreuer] Wöhnert, Heinz Dieter [Akademischer Betreuer] Osiewacz, and Micheala [Akademischer Betreuer] Müller-McNicoll. "Identification of novel base methyltransferases of the 25S rRNA in Saccharomyces cerevisiae / Sunny Sharma. Gutachter: Karl-Dieter Entain ; Jens Wöhnert ; Heinz Dieter Osiewacz ; Micheala Müller-McNicoll." Frankfurt am Main : Univ.-Bibliothek Frankfurt am Main, 2014. http://d-nb.info/1062604032/34.

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Schillewaert, Stéphanie. "Etude de la maturation et de l'assemblage du ribosome eucaryote: caractérisation fonctionnelle de nouveaux facteurs trans-." Doctoral thesis, Universite Libre de Bruxelles, 2011. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/209826.

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La synthèse du ribosome est un processus compliqué, très hiérarchisé et essentiel à toutes les cellules vivantes. La complexité de ce processus tient notamment au fait que les différentes étapes de la biogenèse du ribosome eucaryote sont temporellement et spatialement organisées dans des compartiments cellulaires différents (le nucléole, le nucléoplasme et le cytoplasme). Il est toutefois connu que le pré-ARNr 35S (le précurseur de trois des quatre ARNr, les ARNr 18S, 5.8S et 25S) est pris en charge dès sa synthèse par des facteurs impliqués dans sa maturation. Ainsi, la formation d’un ribosom
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Hang, Pei Chun. "Investigations into Streptomyces azureus Thiostrepton-resistance rRNA Methyltransferase and its Cognate Antibiotic." Thesis, 2008. http://hdl.handle.net/10012/4143.

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Thiostrepton (TS: TS; C72H85N19O18S5) is a thiazoline antibiotic that is effective against Gram-positive bacteria and the malarial parasite, Plasmodium falciparum. Tight binding of TS to the bacterial L11-23S ribosomal RNA (rRNA) complex of the large 50S ribosomal unit inhibits protein biosynthesis. The TS producing organism, Streptomyces azureus, biosynthesizes thiostrepton-resistance methyltransferase (TSR), an enzyme that uses S-adenosyl-L-methionine (AdoMet) as a methyl donor, to modify the TS target site. Methylation of A1067 (Escherichia coli ribosome numbering) by TSR circumvents TS bin
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Kovalic, David Karel. "Methylation of minimalist 23S rRNA sequences in vitro by ErmSF (TlrA) N-methyltransferase." 1997. http://catalog.hathitrust.org/api/volumes/oclc/40100371.html.

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Thesis (Ph. D.)--University of Wisconsin--Madison, 1997.<br>Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 168-191).
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Dey, Debayan. "Crystal Structures of Native and AdoMet Bound rRNA Methyltransferase from Sinorhizobium meliloti : Structural Insights into rRNA Recognition. Evolutionary, Structural and Functional Studies on Nucleoid-Associated Proteins HU and IHF." Thesis, 2016. http://etd.iisc.ac.in/handle/2005/4062.

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DNA- and RNA-binding proteins play a central role in gene regulation, which includes transcriptional control, alternative splicing, post-translational and transcriptional modifications like methylation and acetylation among other roles. In this way, they control most of the working machinery of the cell in direct or indirect manner. Although more than 60 years ago the structure of DNA was proposed by Watson and Crick, our understanding of how RNA- and DNA-binding proteins interact with the genome and transcriptome remains scarce. One of the most important questions in biology is how a large nu
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Treede, Irina [Verfasser]. "Aufklärung der Funktion von zwei rRNA-Methyltransferasen und Untersuchungen zur Eurekanat-Biosynthese in Streptomyces viridochromogenes Tü57 / vorgelegt von Irina Treede." 2004. http://d-nb.info/973266686/34.

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Book chapters on the topic "RRNA Methyltransferase"

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Schomburg, Dietmar, and Dörte Stephan. "rRNA (adenine-N6-)-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_46.

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Schomburg, Dietmar, and Dörte Stephan. "rRNA (guanine-N1-)-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_49.

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Schomburg, Dietmar, and Dörte Stephan. "rRNA (guanine-N2-)-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_50.

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Schomburg, Dietmar, and Dörte Stephan. "rRNA (adenosine-2′-O-)-methyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_63.

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Schomburg, Dietmar, and Ida Schomburg. "16S rRNA (guanine1207-N2)-methyltransferase 2.1.1.172." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_10.

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Schomburg, Dietmar, and Ida Schomburg. "23S rRNA (guanine2445-N2)-methyltransferase 2.1.1.173." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_11.

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Schomburg, Dietmar, and Ida Schomburg. "23S rRNA (guanine1835-N2)-methyltransferase 2.1.1.174." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_12.

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Schomburg, Dietmar, and Ida Schomburg. "16S rRNA (cytosine967-C5)-methyltransferase 2.1.1.176." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_14.

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Schomburg, Dietmar, and Ida Schomburg. "23S rRNA (pseudouridine1915-N3)-methyltransferase 2.1.1.177." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_15.

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Schomburg, Dietmar, and Ida Schomburg. "16S rRNA (cytosine1407-C5)-methyltransferase 2.1.1.178." In Class 2–3.2 Transferases, Hydrolases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_16.

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