RNA polymerase rifampicin resistance mutations in Escherichia coli: Sequence changes and dominance

Ovchinnikov, Yuri A.; Monastyrskaya, G.S.; Guriev, Sergei O.; Kalinina, Nadezhda F.; Свердлов, Е. Д.; Gragerov, Alexander; Bass, I. A.; Kiver, Irina F.; Moiseyeva, Elena P.; Igumnov, Vladimir N.; Mindlin, S. Z.; Nikiforov, Vadim; Khesin, R. B.

doi:10.1007/bf00330662

Cited by 103 publications

(64 citation statements)

References 19 publications

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“…We decided to study the contribution of the MutY protein to A ⅐ T3G ⅐ C mutations that can arise via an A ⅐ C mispair by using the previously described E. coli rpoB/Rif r system to monitor mutations (7). We have extended the work of others (8,19,(22)(23)(24) to generate a system that can analyze 69 different base substitutions in the rpoB gene (7). Recent work (20; E. Wolff, M. Kim, and J. H. Miller, unpublished data) has added several sites to this collection, so that as many as 73 different base substitutions can be monitored by analyzing E. coli Rif r mutants at 37°C (Table 1).…”

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confidence: 99%

Competition between MutY and Mismatch Repair at A · C Mispairs In Vivo

2003

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We show that the MutY protein competes with the MutS-dependent mismatch repair system to process at least some A ⅐ C mispairs in vivo, converting them to G ⅐ C pairs. In the presence of an increased dCTP pool resulting from the loss of nucleotide diphosphate kinase, the frequency of A ⅐ T3G ⅐ C transitions at a hot spot in the rpoB gene is 30-fold lower in a MutY-deficient derivative than in the wild type.

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confidence: 99%

Competition between MutY and Mismatch Repair at A · C Mispairs In Vivo

2003

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“…It is important to note that a significant number of mutations listed in the catalogue (see Table S2 in the supplemental material) have not been described in this article (2,45,46,49,66,67,73,78,80,84,88,91,97,108,111,112,124,126,129,130,146,151,157,160,165,167,168,170,177,180,181,186,193,204). For most of them, only in vivo phenotypes have been described and no in vitro characterization has yet been performed.…”

Section: Discussionmentioning

confidence: 99%

“…8B). More specifically, they are found in the protrusion, fork and external 1 and 2 domains of ␤ (14,31,81,82,97,108,120,127,129,130,156,160,174,178,186,201,202,207). Thus, these replacements most probably affect the conformation of the binding pocket and lower its affinity for rifampin.…”

Section: Drug-resistant Rnap Mutantsmentioning

confidence: 99%

Structural Perspective on Mutations Affecting the Function of Multisubunit RNA Polymerases

Trinh

Langelier

Archambault

et al. 2006

Microbiol Mol Biol Rev

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SUMMARY High-resolution crystallographic structures of multisubunit RNA polymerases (RNAPs) have increased our understanding of transcriptional mechanisms. Based on a thorough review of the literature, we have compiled the mutations affecting the function of multisubunit RNA polymerases, many of which having been generated and studied prior to the publication of the first high-resolution structure, and highlighted the positions of the altered amino acids in the structures of both the prokaryotic and eukaryotic enzymes. The observations support many previous hypotheses on the transcriptional process, including the implication of the bridge helix and the trigger loop in the processivity of RNAP, the importance of contacts between the RNAP jaw-lobe module and the downstream DNA in the establishment of a transcription bubble and selection of the transcription start site, the destabilizing effects of ppGpp on the open promoter complex, and the link between RNAP processivity and termination. This study also revealed novel, remarkable features of the RNA polymerase catalytic mechanisms that will require additional investigation, including the putative roles of fork loop 2 in the establishment of a transcription bubble, the trigger loop in start site selection, and the uncharacterized funnel domain in RNAP processivity.

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“…The sequence of wildtype DNA has been reported (9) only for the EcoRI-generated internal fragment of rpoB, basepairs 3528 through 6401 (Fig.1). ( We use the Post et al scale (1) as corrected in (2), and adjusted for two other discrepancies discussed below).…”

Section: Introductionmentioning

confidence: 99%

The wild-type nucleotide sequence of therpoBC-attenuator region ofEscherichia coliDNA, and its implications for the nature of therif^d18 mutation

Morgan¹,

Kellett²,

Hayward³

1984

Nucl Acids Res

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To investigate the possibility that the unusual dominant rifampicinresistance characteristic of the rifd18 allele of E.coli rpoB is due to a secondary, regulatory mutation, we have determined the nucleotide sequence of a 1.1 Kbp wild-type DNA fragment, including the transcriptional attenuator and translational start-site of r We have also re-investigated the previously published sequences of this region in xrifdl8 and xrifd47 DNA. Our results indicate that all three sequences are identical, and reveal some errors in the published data. We discuss the basis of dominance of rifd18.

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RNA polymerase rifampicin resistance mutations in Escherichia coli: Sequence changes and dominance

Cited by 103 publications

References 19 publications

Competition between MutY and Mismatch Repair at A · C Mispairs In Vivo

Competition between MutY and Mismatch Repair at A · C Mispairs In Vivo

Structural Perspective on Mutations Affecting the Function of Multisubunit RNA Polymerases

The wild-type nucleotide sequence of therpoBC-attenuator region ofEscherichia coliDNA, and its implications for the nature of therif^d18 mutation

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RNA polymerase rifampicin resistance mutations in Escherichia coli: Sequence changes and dominance

Cited by 103 publications

References 19 publications

Competition between MutY and Mismatch Repair at A · C Mispairs In Vivo

Competition between MutY and Mismatch Repair at A · C Mispairs In Vivo

Structural Perspective on Mutations Affecting the Function of Multisubunit RNA Polymerases

The wild-type nucleotide sequence of therpoBC-attenuator region ofEscherichia coliDNA, and its implications for the nature of therifd18 mutation

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Product

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The wild-type nucleotide sequence of therpoBC-attenuator region ofEscherichia coliDNA, and its implications for the nature of therif^d18 mutation