Log in

Relevant bibliographies by topics / RRNA Methyltransferase / Journal articles

To see the other types of publications on this topic, follow the link: RRNA Methyltransferase.

Journal articles on the topic 'RRNA Methyltransferase'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'RRNA Methyltransferase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

11

Wachino, Jun-ichi, Keigo Shibayama, Hiroshi Kurokawa, et al. "Novel Plasmid-Mediated 16S rRNA m1A1408 Methyltransferase, NpmA, Found in a Clinically Isolated Escherichia coli Strain Resistant to Structurally Diverse Aminoglycosides." Antimicrobial Agents and Chemotherapy 51, no. 12 (2007): 4401–9. http://dx.doi.org/10.1128/aac.00926-07.

Full text

Abstract:

ABSTRACT We have isolated a multiple-aminoglycoside-resistant Escherichia coli strain, strain ARS3, and have been the first to identify a novel plasmid-mediated 16S rRNA methyltransferase, NpmA. This new enzyme shared a relatively low level of identity (30%) to the chromosomally encoded 16S rRNA methyltransferase (KamA) of Streptomyces tenjimariensis, an actinomycete aminoglycoside producer. The introduction of a recombinant plasmid carrying npmA could confer on E. coli consistent resistance to both 4,6-disubstituted 2-deoxystreptamines, such as amikacin and gentamicin, and 4,5-disubstituted 2

APA, Harvard, Vancouver, ISO, and other styles

12

Zhu, Chengming, Qi Yan, Chenchun Weng, et al. "Erroneous ribosomal RNAs promote the generation of antisense ribosomal siRNA." Proceedings of the National Academy of Sciences 115, no. 40 (2018): 10082–87. http://dx.doi.org/10.1073/pnas.1800974115.

Full text

Abstract:

Ribosome biogenesis is a multistep process, during which mistakes can occur at any step of pre-rRNA processing, modification, and ribosome assembly. Misprocessed rRNAs are usually detected and degraded by surveillance machineries. Recently, we identified a class of antisense ribosomal siRNAs (risiRNAs) that down-regulate pre-rRNAs through the nuclear RNAi pathway. To further understand the biological roles of risiRNAs, we conducted both forward and reverse genetic screens to search for more suppressor of siRNA (susi) mutants. We isolated a number of genes that are broadly conserved from yeast

APA, Harvard, Vancouver, ISO, and other styles

13

Gutierrez, Belen, Jose A. Escudero, Alvaro San Millan, et al. "Fitness Cost and Interference of Arm/Rmt Aminoglycoside Resistance with the RsmF Housekeeping Methyltransferases." Antimicrobial Agents and Chemotherapy 56, no. 5 (2012): 2335–41. http://dx.doi.org/10.1128/aac.06066-11.

Full text

Abstract:

ABSTRACTArm/Rmt methyltransferases have emerged recently in pathogenic bacteria as enzymes that confer high-level resistance to 4,6-disubstituted aminoglycosides through methylation of the G1405 residue in the 16S rRNA (like ArmA and RmtA to -E). In prokaryotes, nucleotide methylations are the most common type of rRNA modification, and they are introduced posttranscriptionally by a variety of site-specific housekeeping enzymes to optimize ribosomal function. Here we show that while the aminoglycoside resistance methyltransferase RmtC methylates G1405, it impedes methylation of the housekeeping

APA, Harvard, Vancouver, ISO, and other styles

14

Husain, Nilofer, Karolina L. Tkaczuk, Rajesh T. Shenoy, et al. "Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m 7 G methyltransferases." Nucleic Acids Research 38, no. 12 (2010): 4120–32. http://dx.doi.org/10.1093/nar/gkq122.

Full text

Abstract:

Abstract Sgm (Sisomicin-gentamicin methyltransferase) from antibiotic-producing bacterium Micromonospora zionensis is an enzyme that confers resistance to aminoglycosides like gentamicin and sisomicin by specifically methylating G1405 in bacterial 16S rRNA. Sgm belongs to the aminoglycoside resistance methyltransferase (Arm) family of enzymes that have been recently found to spread by horizontal gene transfer among disease-causing bacteria. Structural characterization of Arm enzymes is the key to understand their mechanism of action and to develop inhibitors that would block their activity. He

APA, Harvard, Vancouver, ISO, and other styles

15

Zou, Meijuan, Ying Mu, Xin Chai, et al. "The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development." Nucleic Acids Research 48, no. 6 (2020): 3195–210. http://dx.doi.org/10.1093/nar/gkaa129.

Full text

Abstract:

Abstract Methylation of nucleotides in ribosomal RNAs (rRNAs) is a ubiquitous feature that occurs in all living organisms. The formation of methylated nucleotides is performed by a variety of RNA-methyltransferases. Chloroplasts of plant cells result from an endosymbiotic event and possess their own genome and ribosomes. However, enzymes responsible for rRNA methylation and the function of modified nucleotides in chloroplasts remain to be determined. Here, we identified an rRNA methyltransferase, CMAL (Chloroplast MraW-Like), in the Arabidopsis chloroplast and investigated its function. CMAL i

APA, Harvard, Vancouver, ISO, and other styles

16

Zong, Zhiyong, Sally R. Partridge, and Jonathan R. Iredell. "RmtC 16S rRNA Methyltransferase in Australia." Antimicrobial Agents and Chemotherapy 52, no. 2 (2007): 794–95. http://dx.doi.org/10.1128/aac.01399-07.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Granier, Sophie A., Laura Hidalgo, Alvaro San Millan, et al. "ArmA Methyltransferase in a Monophasic Salmonella enterica Isolate from Food." Antimicrobial Agents and Chemotherapy 55, no. 11 (2011): 5262–66. http://dx.doi.org/10.1128/aac.00308-11.

Full text

Abstract:

ABSTRACTThe 16S rRNA methyltransferase ArmA is a worldwide emerging determinant that confers high-level resistance to most clinically relevant aminoglycosides. We report here the identification and characterization of a multidrug-resistantSalmonella entericasubspecies I.4,12:i:− isolate recovered from chicken meat sampled in a supermarket on February 2009 in La Reunion, a French island in the Indian Ocean. Susceptibility testing showed an unusually high-level resistance to gentamicin, as well as to ampicillin, expanded-spectrum cephalosporins and amoxicillin-clavulanate. Molecular analysis of

APA, Harvard, Vancouver, ISO, and other styles

18

Hopkins, Katie L., Jose A. Escudero, Laura Hidalgo, and Bruno Gonzalez-Zorn. "16S rRNA Methyltransferase RmtC inSalmonella entericaSerovar Virchow." Emerging Infectious Diseases 16, no. 4 (2010): 712–15. http://dx.doi.org/10.3201/eid1604.090736.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Richter, Uwe, Kristina Kühn, Sachiko Okada, Axel Brennicke, Andreas Weihe, and Thomas Börner. "A mitochondrial rRNA dimethyladenosine methyltransferase in Arabidopsis." Plant Journal 61, no. 4 (2010): 558–69. http://dx.doi.org/10.1111/j.1365-313x.2009.04079.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Gupta, Kirti, Ankit Gupta, and Saman Habib. "Characterization of a Plasmodium falciparum rRNA methyltransferase." Molecular and Biochemical Parasitology 223 (July 2018): 13–18. http://dx.doi.org/10.1016/j.molbiopara.2018.06.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Xu, Zhili, Heather C. O'Farrell, Jason P. Rife, and Gloria M. Culver. "A conserved rRNA methyltransferase regulates ribosome biogenesis." Nature Structural & Molecular Biology 15, no. 5 (2008): 534–36. http://dx.doi.org/10.1038/nsmb.1408.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Tomikawa, Chie. "7-Methylguanosine Modifications in Transfer RNA (tRNA)." International Journal of Molecular Sciences 19, no. 12 (2018): 4080. http://dx.doi.org/10.3390/ijms19124080.

Full text

Abstract:

More than 90 different modified nucleosides have been identified in tRNA. Among the tRNA modifications, the 7-methylguanosine (m7G) modification is found widely in eubacteria, eukaryotes, and a few archaea. In most cases, the m7G modification occurs at position 46 in the variable region and is a product of tRNA (m7G46) methyltransferase. The m7G46 modification forms a tertiary base pair with C13-G22, and stabilizes the tRNA structure. A reaction mechanism for eubacterial tRNA m7G methyltransferase has been proposed based on the results of biochemical, bioinformatic, and structural studies. How

APA, Harvard, Vancouver, ISO, and other styles

23

Militello, Kevin T., Jennifer Leigh, Matthew Pusateri, Laurie K. Read, and Dineen Vogler. "A role for a Trypanosoma brucei cytosine RNA methyltransferase homolog in ribosomal RNA processing." PLOS ONE 19, no. 4 (2024): e0298521. http://dx.doi.org/10.1371/journal.pone.0298521.

Full text

Abstract:

In Trypanosoma brucei, gene expression is primarily regulated posttranscriptionally making RNA metabolism critical. T. brucei has an epitranscriptome containing modified RNA bases. Yet, the identity of the enzymes catalyzing modified RNA base addition and the functions of the enzymes and modifications remain unclear. Homology searches indicate the presence of numerous T. brucei cytosine RNA methyltransferase homologs. One such homolog, TbNop2 was studied in detail. TbNop2 contains the six highly conserved motifs found in cytosine RNA methyltransferases and is evolutionarily related to the Nop2

APA, Harvard, Vancouver, ISO, and other styles

24

Abedeera, Sudeshi M., Caitlin M. Hawkins, and Sanjaya C. Abeysirigunawardena. "RsmG forms stable complexes with premature small subunit rRNA during bacterial ribosome biogenesis." RSC Advances 10, no. 38 (2020): 22361–69. http://dx.doi.org/10.1039/d0ra02732d.

Full text

Abstract:

RsmG is the methyltransferase responsible for the N7 methylation of G527 of 16S rRNA. Here we show that RsmG binds preferably to premature bacterial small subunit rRNA. The presence of ribosomal proteins also influences the stability of RsmG–rRNA complexes.

APA, Harvard, Vancouver, ISO, and other styles

25

Inoue, Koichi, Soumit Basu, and Masayori Inouye. "Dissection of 16S rRNA Methyltransferase (KsgA) Function in Escherichia coli." Journal of Bacteriology 189, no. 23 (2007): 8510–18. http://dx.doi.org/10.1128/jb.01259-07.

Full text

Abstract:

ABSTRACT A 16S rRNA methyltransferase, KsgA, identified originally in Escherichia coli is highly conserved in all living cells, from bacteria to humans. KsgA orthologs in eukaryotes possess functions in addition to their rRNA methyltransferase activity. E. coli Era is an essential GTP-binding protein. We recently observed that KsgA functions as a multicopy suppressor for the cold-sensitive cell growth of an era mutant [Era(E200K)] strain (Q. Lu and M. Inouye, J. Bacteriol. 180:5243-5246, 1998). Here we observed that although KsgA(E43A), KsgA(G47A), and KsgA(E66A) mutations located in the S-ade

APA, Harvard, Vancouver, ISO, and other styles

26

Dunn, Sianadh, Olivia Lombardi, and Victoria H. Cowling. "c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production." Biochemical Journal 474, no. 3 (2017): 377–84. http://dx.doi.org/10.1042/bcj20160930.

Full text

Abstract:

The mRNA cap is a structure added to RNA pol II transcripts in eukaryotes, which recruits factors involved in RNA processing, nuclear export and translation initiation. RNA guanine-7 methyltransferase (RNMT)–RNA-activating miniprotein (RAM), the mRNA cap methyltransferase complex, completes the basic functional mRNA cap structure, cap 0, by methylating the cap guanosine. Here, we report that RNMT–RAM co-ordinates mRNA processing with ribosome production. Suppression of RNMT–RAM reduces synthesis of the 45S ribosomal RNA (rRNA) precursor. RNMT–RAM is required for c-Myc expression, a major regul

APA, Harvard, Vancouver, ISO, and other styles

27

Atkinson, Gemma C., Lykke H. Hansen, Tanel Tenson, Anette Rasmussen, Finn Kirpekar, and Birte Vester. "Distinction between the Cfr Methyltransferase Conferring Antibiotic Resistance and the Housekeeping RlmN Methyltransferase." Antimicrobial Agents and Chemotherapy 57, no. 8 (2013): 4019–26. http://dx.doi.org/10.1128/aac.00448-13.

Full text

Abstract:

ABSTRACTThecfrgene encodes the Cfr methyltransferase that primarily methylates C-8 in A2503 of 23S rRNA in the peptidyl transferase region of bacterial ribosomes. The methylation provides resistance to six classes of antibiotics of clinical and veterinary importance. TherlmNgene encodes the RlmN methyltransferase that methylates C-2 in A2503 in 23S rRNA and A37 in tRNA, but RlmN does not significantly influence antibiotic resistance. The enzymes are homologous and use the same mechanism involving radicalS-adenosyl methionine to methylate RNA via an intermediate involving a methylated cysteine

APA, Harvard, Vancouver, ISO, and other styles

28

Sergeeva, Olga, Philipp Sergeev, Pavel Melnikov, Tatiana Prikazchikova, Olga Dontsova, and Timofei Zatsepin. "Modification of Adenosine196 by Mettl3 Methyltransferase in the 5’-External Transcribed Spacer of 47S Pre-rRNA Affects rRNA Maturation." Cells 9, no. 4 (2020): 1061. http://dx.doi.org/10.3390/cells9041061.

Full text

Abstract:

Ribosome biogenesis is among the founding processes in the cell. During the first stages of ribosome biogenesis, polycistronic precursor of ribosomal RNA passes complex multistage maturation after transcription. Quality control of preribosomal RNA (pre-rRNA) processing is precisely regulated by non-ribosomal proteins and structural features of pre-rRNA molecules, including modified nucleotides. However, many participants of rRNA maturation are still unknown or poorly characterized. We report that RNA m6A methyltransferase Mettl3 interacts with the 5′ external transcribed spacer (5′ETS) of the

APA, Harvard, Vancouver, ISO, and other styles

29

Bueno, Maria Fernanda C., Gabriela R. Francisco, Jessica A. O'Hara, Doroti de Oliveira Garcia та Yohei Doi. "Coproduction of 16S rRNA Methyltransferase RmtD or RmtG with KPC-2 and CTX-M Group Extended-Spectrum β-Lactamases in Klebsiella pneumoniae". Antimicrobial Agents and Chemotherapy 57, № 5 (2013): 2397–400. http://dx.doi.org/10.1128/aac.02108-12.

Full text

Abstract:

ABSTRACTEightKlebsiella pneumoniaeclinical strains with high-level aminoglycoside resistance were collected from eight hospitals in São Paulo State, Brazil, in 2010 and 2011. Three of them produced an RmtD group 16S rRNA methyltransferase, RmtD1 or RmtD2. Five strains were found to produce a novel 16S rRNA methyltransferase, designated RmtG, which shared 57 to 58% amino acid identity with RmtD1 and RmtD2. Seven strains coproduced KPC-2 with or without various CTX-M group extended-spectrum β-lactamases, while the remaining strain coproduced CTX-M-2.

APA, Harvard, Vancouver, ISO, and other styles

30

Hager, Jutta, Bart L. Staker, and Ursula Jakob. "Substrate Binding Analysis of the 23S rRNA Methyltransferase RrmJ." Journal of Bacteriology 186, no. 19 (2004): 6634–42. http://dx.doi.org/10.1128/jb.186.19.6634-6642.2004.

Full text

Abstract:

ABSTRACT The 23S rRNA methyltransferase RrmJ (FtsJ) is responsible for the 2′-O methylation of the universally conserved U2552 in the A loop of 23S rRNA. This 23S rRNA modification appears to be critical for ribosome stability, because the absence of functional RrmJ causes the cellular accumulation of the individual ribosomal subunits at the expense of the functional 70S ribosomes. To gain insight into the mechanism of substrate recognition for RrmJ, we performed extensive site-directed mutagenesis of the residues conserved in RrmJ and characterized the mutant proteins both in vivo and in vitr

APA, Harvard, Vancouver, ISO, and other styles

31

McCulloch, Vicki, and Gerald S. Shadel. "Human Mitochondrial Transcription Factor B1 Interacts with the C-Terminal Activation Region of h-mtTFA and Stimulates Transcription Independently of Its RNA Methyltransferase Activity." Molecular and Cellular Biology 23, no. 16 (2003): 5816–24. http://dx.doi.org/10.1128/mcb.23.16.5816-5824.2003.

Full text

Abstract:

ABSTRACT A significant advancement in understanding mitochondrial gene expression is the recent identification of two new human mitochondrial transcription factors, h-mtTFB1 and h-mtTFB2. Both proteins stimulate transcription in collaboration with the high-mobility group box transcription factor, h-mtTFA, and are homologous to rRNA methyltransferases. In fact, the dual-function nature of h-mtTFB1 was recently demonstrated by its ability to methylate a conserved rRNA substrate. Here, we demonstrate that h-mtTFB1 binds h-mtTFA both in HeLa cell mitochondrial extracts and in direct-binding assays

APA, Harvard, Vancouver, ISO, and other styles

32

Lövgren, J. Mattias, and P. Mikael Wikström. "The rlmB Gene Is Essential for Formation of Gm2251 in 23S rRNA but Not for Ribosome Maturation inEscherichia coli." Journal of Bacteriology 183, no. 23 (2001): 6957–60. http://dx.doi.org/10.1128/jb.183.23.6957-6960.2001.

Full text

Abstract:

ABSTRACT In Saccharomyces cerevisiae, the rRNA Gm2270 methyltransferase, Pet56p, has an essential role in the maturation of the mitochondrial large ribosomal subunit that is independent of its methyltransferase activity. Here we show that the proposedEscherichia coli ortholog, RlmB (formerly YjfH), indeed is essential for the formation of Gm in position 2251 of 23S rRNA. However, a ΔrlmB mutant did not show any ribosome assembly defects and was not outgrown by a wild-type strain even after 120 cell mass doublings. Thus, RlmB has no important role in ribosome assembly or function in E. coli.

APA, Harvard, Vancouver, ISO, and other styles

33

Sharkey, Rory E., Johnny B. Herbert, Danielle A. McGaha, Vy Nguyen, Allyn J. Schoeffler, and Jack A. Dunkle. "Three critical regions of the erythromycin resistance methyltransferase, ErmE, are required for function supporting a model for the interaction of Erm family enzymes with substrate rRNA." RNA 28, no. 2 (2021): 210–26. http://dx.doi.org/10.1261/rna.078946.121.

Full text

Abstract:

6-Methyladenosine modification of DNA and RNA is widespread throughout the three domains of life and often accomplished by a Rossmann-fold methyltransferase domain which contains conserved sequence elements directing S-adenosylmethionine cofactor binding and placement of the target adenosine residue into the active site. Elaborations to the conserved Rossman-fold and appended domains direct methylation to diverse DNA and RNA sequences and structures. Recently, the first atomic-resolution structure of a ribosomal RNA adenine dimethylase (RRAD) family member bound to rRNA was solved, TFB1M bound

APA, Harvard, Vancouver, ISO, and other styles

34

Farrow, Kylie A., Dena Lyras, Galina Polekhina, Katerina Koutsis, Michael W. Parker, and Julian I. Rood. "Identification of Essential Residues in the Erm(B) rRNA Methyltransferase of Clostridium perfringens." Antimicrobial Agents and Chemotherapy 46, no. 5 (2002): 1253–61. http://dx.doi.org/10.1128/aac.46.5.1253-1261.2002.

Full text

Abstract:

ABSTRACT Macrolide-lincosamide-streptogramin B resistance is widespread, with the determinants encoding resistance to antibiotics such as erythromycin being detected in many bacterial pathogens. Resistance is most commonly mediated by the production of an Erm protein, a 23S rRNA methyltransferase. We have undertaken a mutational analysis of the Erm(B) protein from Clostridium perfringens with the objective of developing a greater understanding of the mechanism of action of this protein. A recombinant plasmid that carried the erm(B) gene was mutated by either in vitro hydroxylamine mutagenesis

APA, Harvard, Vancouver, ISO, and other styles

35

Kumar, Atul, Santosh Kumar, and Bhupesh Taneja. "The structure of Rv2372c identifies an RsmE-like methyltransferase fromMycobacterium tuberculosis." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (2014): 821–32. http://dx.doi.org/10.1107/s1399004713033555.

Full text

Abstract:

U1498 of 16S rRNA plays an important role in translation fidelity as well as in antibiotic response. U1498 is present in a methylated form in the decoding centre of the ribosome. In this study, Rv2372c fromMycobacterium tuberculosishas been identified as an RsmE-like methyltransferase which specifically methylates U1498 of 16S rRNA at the N3 position and can complement RsmE-deletedEscherichia coli. The crystal structure of Rv2372c has been determined, and reveals that the protein belongs to a distinct class in the SPOUT superfamily and exists as a dimer. The deletion of critical residues at th

APA, Harvard, Vancouver, ISO, and other styles

36

Fritsche, Thomas R., Mariana Castanheira, George H. Miller, Ronald N. Jones, and Eliana S. Armstrong. "Detection of Methyltransferases Conferring High-Level Resistance to Aminoglycosides in Enterobacteriaceae from Europe, North America, and Latin America." Antimicrobial Agents and Chemotherapy 52, no. 5 (2008): 1843–45. http://dx.doi.org/10.1128/aac.01477-07.

Full text

Abstract:

ABSTRACT The alteration of ribosomal targets by recently described 16S rRNA methyltransferases confers resistance to most aminoglycosides, including arbekacin. Enterobacteriaceae and nonfermentative bacilli acquired through global surveillance programs were screened for the presence of these enzymes on the basis of phenotypes that were resistant to nine tested aminoglycosides. Subsequent molecular studies determined that 20 of 21 (95.2%) methyltransferase-positive isolates consisted of novel species records or geographic occurrences (North America [armA and rmtB], Latin America [rmtD], and Eur

APA, Harvard, Vancouver, ISO, and other styles

37

Sergeeva, O. V., D. E. Burakovsky, P. V. Sergiev, et al. "Usage of rRNA-methyltransferase for site-specific fluorescent labeling." Moscow University Chemistry Bulletin 67, no. 2 (2012): 88–93. http://dx.doi.org/10.3103/s0027131412020058.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Kita, S., I. Tanaka, M. Yao, and Y. Tanaka. "Structural and functional analysis of rRNA methyltransferase fromStaphylococcus aureus." Acta Crystallographica Section A Foundations of Crystallography 67, a1 (2011): C435—C436. http://dx.doi.org/10.1107/s0108767311089069.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Mann, Paul A., Liqun Xiong, Alexander S. Mankin, et al. "EmtA, a rRNA methyltransferase conferring high-level evernimicin resistance." Molecular Microbiology 41, no. 6 (2001): 1349–56. http://dx.doi.org/10.1046/j.1365-2958.2001.02602.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Pintard, L. "MRM2 encodes a novel yeast mitochondrial 21S rRNA methyltransferase." EMBO Journal 21, no. 5 (2002): 1139–47. http://dx.doi.org/10.1093/emboj/21.5.1139.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Gu, Xiang Rong, Claes Gustafsson, Jung Ku, Ming Yu, and Daniel V. Santi. "Identification of the 16S rRNA m5C967 Methyltransferase fromEscherichia coli†." Biochemistry 38, no. 13 (1999): 4053–57. http://dx.doi.org/10.1021/bi982364y.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Su, Sai L., and David Dubnau. "Binding of Bacillus subtilis ermC' methyltransferase to 23S rRNA." Biochemistry 29, no. 25 (1990): 6033–42. http://dx.doi.org/10.1021/bi00477a022.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Weitnauer, Gabriele, Sibylle Gaisser, Axel Trefzer, et al. "An ATP-Binding Cassette Transporter and Two rRNA Methyltransferases Are Involved in Resistance to Avilamycin in the Producer Organism Streptomyces viridochromogenesTü57." Antimicrobial Agents and Chemotherapy 45, no. 3 (2001): 690–95. http://dx.doi.org/10.1128/aac.45.3.690-695.2001.

Full text

Abstract:

ABSTRACT Three different resistance factors from the avilamycin biosynthetic gene cluster of Streptomyces viridochromogenes Tü57, which confer avilamycin resistance when expressed in Streptomyces lividans TK66, were isolated. Analysis of the deduced amino acid sequences showed that AviABC1 is similar to a large family of ATP-binding transporter proteins and that AviABC2 resembles hydrophobic transmembrane proteins known to act jointly with the ATP-binding proteins. The deduced amino acid sequence of aviRb showed similarity to those of other rRNA methyltransferases, and AviRa did not resemble

APA, Harvard, Vancouver, ISO, and other styles

44

Lyu, Guoliang, Le Zong, Chao Zhang, et al. "Metastasis-related methyltransferase 1 (Merm1) represses the methyltransferase activity of Dnmt3a and facilitates RNA polymerase I transcriptional elongation." Journal of Molecular Cell Biology 11, no. 1 (2018): 78–90. http://dx.doi.org/10.1093/jmcb/mjy023.

Full text

Abstract:

Abstract Stimulatory regulators for DNA methyltransferase activity, such as Dnmt3L and some Dnmt3b isoforms, affect DNA methylation patterns, thereby maintaining gene body methylation and maternal methylation imprinting, as well as the methylation landscape of pluripotent cells. Here we show that metastasis-related methyltransferase 1 (Merm1), a protein deleted in individuals with Williams–Beuren syndrome, acts as a repressive regulator of Dnmt3a. Merm1 interacts with Dnmt3a and represses its methyltransferase activity with the requirement of the binding motif for S-adenosyl-L-methionine. Func

APA, Harvard, Vancouver, ISO, and other styles

45

Long, Katherine S., Jacob Poehlsgaard, Corinna Kehrenberg, Stefan Schwarz, and Birte Vester. "The Cfr rRNA Methyltransferase Confers Resistance to Phenicols, Lincosamides, Oxazolidinones, Pleuromutilins, and Streptogramin A Antibiotics." Antimicrobial Agents and Chemotherapy 50, no. 7 (2006): 2500–2505. http://dx.doi.org/10.1128/aac.00131-06.

Full text

Abstract:

ABSTRACT A novel multidrug resistance phenotype mediated by the Cfr rRNA methyltransferase is observed in Staphylococcus aureus and Escherichia coli. The cfr gene has previously been identified as a phenicol and lincosamide resistance gene on plasmids isolated from Staphylococcus spp. of animal origin and recently shown to encode a methyltransferase that modifies 23S rRNA at A2503. Antimicrobial susceptibility testing shows that S. aureus and E. coli strains expressing the cfr gene exhibit elevated MICs to a number of chemically unrelated drugs. The phenotype is named PhLOPSA for resistance to

APA, Harvard, Vancouver, ISO, and other styles

46

Gustafsson, Claes, and Britt C. Persson. "Identification of the rrmA Gene Encoding the 23S rRNA m1G745 Methyltransferase in Escherichia coli and Characterization of an m1G745-Deficient Mutant." Journal of Bacteriology 180, no. 2 (1998): 359–65. http://dx.doi.org/10.1128/jb.180.2.359-365.1998.

Full text

Abstract:

ABSTRACT An Escherichia coli mutant lacking the modified nucleotide m1G in rRNA has previously been isolated (G. R. Björk and L. A. Isaksson, J. Mol. Biol. 51:83–100, 1970). In this study, we localize the position of the m1G to nucleotide 745 in 23S rRNA and characterize a mutant deficient in this modification. This mutant shows a 40% decreased growth rate in rich media, a drastic reduction in loosely coupled ribosomes, a 20% decreased polypeptide chain elongation rate, and increased resistance to the ribosome binding antibiotic viomycin. TherrmA gene encoding 23S rRNA m1G745 methyltransferas

APA, Harvard, Vancouver, ISO, and other styles

47

Smith, Lisa K., and Alexander S. Mankin. "Transcriptional and Translational Control of the mlr Operon, Which Confers Resistance to Seven Classes of Protein Synthesis Inhibitors." Antimicrobial Agents and Chemotherapy 52, no. 5 (2008): 1703–12. http://dx.doi.org/10.1128/aac.01583-07.

Full text

Abstract:

ABSTRACT The methyltransferase genes erm(B) and cfr are adjacent to each other in the chromosome of methicillin-resistant Staphylococcus aureus strain CM05. Analyses of the transcriptional organization of the erm(B) and cfr genes in the chromosome of strain CM05 showed that the two genes are organized into an operon, designated mlr (for modification of the large ribosomal subunit), which is controlled by the erm(B) promoter. Analysis of the translation control and the inducibility of the erm(B) and cfr genes in the mlr operon showed that despite the presence of putative regulatory short open r

APA, Harvard, Vancouver, ISO, and other styles

48

Douthwaite, Stephen, Bjørn Voldborg, Lykke Haastrup Hansen, Gunnar Rosendahl, and Birte Vester. "Recognition determinants for proteins and antibiotics within 23S rRNA." Biochemistry and Cell Biology 73, no. 11-12 (1995): 1179–85. http://dx.doi.org/10.1139/o95-127.

Full text

Abstract:

Ribosomal RNAs fold into phylogenetically conserved secondary and tertiary structures that determine their function in protein synthesis. We have investigated Escherichia coli 23S rRNA to identify structural elements that interact with antibiotic and protein ligands. Using a combination of molecular genetic and biochemical probing techniques, we have concentrated on regions of the rRNA that are connected with specific functions. These are located in different domains within the 23S rRNA and include the ribosomal GTPase-associated center in domain II, which contains the binding sites for r-prot

APA, Harvard, Vancouver, ISO, and other styles

49

Stephan, Niklas C., Anne B. Ries, Daniel Boehringer, and Nenad Ban. "Structural basis of successive adenosine modifications by the conserved ribosomal methyltransferase KsgA." Nucleic Acids Research 49, no. 11 (2021): 6389–98. http://dx.doi.org/10.1093/nar/gkab430.

Full text

Abstract:

Abstract Biogenesis of ribosomal subunits involves enzymatic modifications of rRNA that fine-tune functionally important regions. The universally conserved prokaryotic dimethyltransferase KsgA sequentially modifies two universally conserved adenosine residues in helix 45 of the small ribosomal subunit rRNA, which is in proximity of the decoding site. Here we present the cryo-EM structure of Escherichia coli KsgA bound to an E. coli 30S at a resolution of 3.1 Å. The high-resolution structure reveals how KsgA recognizes immature rRNA and binds helix 45 in a conformation where one of the substrat

APA, Harvard, Vancouver, ISO, and other styles

50

Pinto, Rita, Cathrine B. Vågbø, Magnus E. Jakobsson, et al. "The human methyltransferase ZCCHC4 catalyses N6-methyladenosine modification of 28S ribosomal RNA." Nucleic Acids Research 48, no. 2 (2019): 830–46. http://dx.doi.org/10.1093/nar/gkz1147.

Full text

Abstract:

Abstract RNA methylations are essential both for RNA structure and function, and are introduced by a number of distinct methyltransferases (MTases). In recent years, N6-methyladenosine (m6A) modification of eukaryotic mRNA has been subject to intense studies, and it has been demonstrated that m6A is a reversible modification that regulates several aspects of mRNA function. However, m6A is also found in other RNAs, such as mammalian 18S and 28S ribosomal RNAs (rRNAs), but the responsible MTases have remained elusive. 28S rRNA carries a single m6A modification, found at position A4220 (alternati

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!