Molecular characterization of Rifr mutations in Pseudomonas aeruginosa and Pseudomonas putida

Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis

Volumn 683, Issue 1-2, 2010, Pages 106-114

  Jatsenko, Tatjana ^a   Tover, Andres ^a   Tegova, Radi ^a   Kivisaar, Maia ^a  

^a UNIVERSITY OF TARTU   (Estonia)

Author keywords

Mutations in rpoB gene; Pseudomonas aeruginosa and Pseudomonas putida; Rifampicin resistance; Temperature effects on spectrum of mutations; Test system for studying mutational processes

Indexed keywords

BACTERIAL PROTEIN; RIFAMPICIN; RIFAMPICIN RESISTANCE PROTEIN; RNA POLYMERASE BETA SUBUNIT; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL GENETICS; BACTERIAL GROWTH; BACTERIUM COLONY; BACTERIUM MUTANT; CONTROLLED STUDY; GENE CLUSTER; GENE MUTATION; GENE SEQUENCE; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; NUCLEIC ACID BASE SUBSTITUTION; PHENOTYPE; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS PUTIDA; TEMPERATURE DEPENDENCE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; DNA-DIRECTED RNA POLYMERASES; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEIC ACID SYNTHESIS INHIBITORS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS PUTIDA; RIFAMPIN; SEQUENCE HOMOLOGY, AMINO ACID; SEQUENCE HOMOLOGY, NUCLEIC ACID;

PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS PUTIDA;

EID: 71549137129     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2009.10.015     Document Type: Article

References (62)

1. Foster P.L. Stress-induced mutagenesis in bacteria. Crit. Rev. Biochem. Mol. Biol. 42 2007 (2007) 373-397
2. Galhardo R.S., Hastings P.J., and Rosenberg S.M. Mutation as a stress response and the regulation of evolvability. Crit. Rev. Biochem. Mol. Biol. 42 (2007) 399-435
3. Couce A., and Blázquez J. Side effects of antibiotics on genetic variability. FEMS Microbiol. 33 (2009) 531-538
4. Taverna P., and Sedgwick B. Generation of an endogenous DNA-methylating agent by nitrosation in Escherichia coli. J. Bacteriol. 178 (1996) 5105-5111
5. Bjelland S., and Seeberg E. Mutagenicity, toxicity and repair of DNA base damage induced by oxidation. Mutat. Res. 531 (2003) 37-80
6. Farabough P.J., Schmeissner U., Hofer M., and Miller J.H. Genetic studies of the lacI repressor. VII. On the molecular nature of spontaneous hotspots in the lacI gene of Escherichia coli. J. Mol. Biol. 126 (1978) 847-863
7. Cupples C.G., and Miller J.H. A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 5345-5349
8. Cupples C.G., Cabrera M., Cruz C., and Miller J.H. A set of lacZ mutations in Escherichia coli that allow rapid detection of specific frameshift mutations. Genetics 125 (1990) 275-280
9. Cairns J., and Foster P.L. Adaptive reversion of a frameshift mutation in Escherichia coli. Genetics 128 (1991) 695-701
10. Schaaper R.M., and Dunn R.L. Spontaneous mutation in the Escherichia coli lacI gene. Genetics (1991) 317-326
11. LeClerc J.E., and Istock N.L. Specificity of UV mutagenesis in the lac promoter of M13lac hybrid phage DNA. Nature 297 (1982) 596-598
12. Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K., Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H., Hancock R.E., Lory S., and Olson M.V. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406 (2000) 959-964
13. Aumeran C., Paillard C., Robin F., Kanold J., Baud O., Bonnet R., Souweine B., and Traore O. Pseudomonas aeruginosa and Pseudomonas putida outbreak associated with contaminated water outlets in an oncohaematology paediatric unit. J. Hosp. Infect. 65 (2007) 47-53
14. Kasak L., Hõrak R., and Kivisaar M. Promoter-creating mutations in Pseudomonas putida: a model system for the study of mutation in starving bacteria. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 3134-3139
15. Tegova R., Tover A., Tarassova K., Tark M., and Kivisaar M. Involvement of error-prone DNA polymerase pol IV on stationary phase mutagenesis in Pseudomonas putida. J. Bacteriol. 186 (2004) 2735-2744
16. Hartmann G., Honikel K.O., Knüsel F., and Nüesch J. The specific inhibition of the DNA-directed RNA synthesis by rifamycin. Biochim. Biophys. Acta 145 (1967) 843-844
17. Campbell E.A., Korzheva N., Mustaev A., Murakami K., Nair S., Goldfarb A., and Darst S.A. Structural mechanism for rifampicin inhibition of bacterial RNA polymerase. Cell (2001) 901-912
18. Ovchinnikov Y.A., Monastyrskaya G.S., Guriev S.O., Kalinina N.F., Sverdlov E.D., Gragerov A.I., Bass I.A., Kiver I.F., Moiseyeva E.P., Igumnov V.M., Mindlin S.Z., Nikiforov V.G., and Khesin R.B. RNA polymerase rifampicin resistance mutations in Escherichia coli: sequence changes and dominance. Mol. Gen. Genet. 190 (1983) 344-348
19. Jin D.J., and Gross C.A. Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance. J. Mol. Biol. 202 (1988) 45-58
20. Severinov K., Soushko M., Goldfarb A., and Nikiforov V. Rifampicin region revisited. J. Biol. Chem. 268 (1993) 14820-14825
21. Artsimovitch I., Vassylyeva M.N., Svetlov D., Svetlov V., Perederina A., Igarashi N., Matsugaki N., Wakatsuki S., Tahirov T.H., and Vassylyev D.G. Allosteric modulation of the RNA polymerase catalytic reaction is an essential component of transcription control by rifamycins. Cell (2005) 351-363
22. Campbell E.A., Pavlova O., Zankin N., Leon F., Irschik H., Jansen R., Severinov K., and Darst S.A. Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase. EMBO J. 24 (2005) 674-682
23. Xu M., Zhou Y.N., Goldstein B.P., and Jin D.J. Cross-resistance of Escherichia coli RNA polymerase conferring rifampin resistance to different antibiotics. J. Bacteriol. 187 (2005) 2783-2792
24. Garibyan L., Huang T., Kim M., Wolff E., Nguyen A., Nguyen T., Diep A., Hu K., Iverson A., Yang H., and Miller J.H. Use of the rpoB gene to determine the specificity of base substitutions on the Escherichia coli chromosome. DNA Repair 2 (2003) 593-608
25. Lisitsyn N.A., Sverdlov E.D., Moiseyeva E.P., Danilevskaya O.N., and Nikiforov V.G. Mutation to rifampicin resistance at the beginning of the RNA polymerase beta subunit gene in Escherichia coli. Mol. Gen. Genet. 196 (1984) 173-174
26. Oliver A., Cantón R., Campo P., Baquero F., and Blázquez J. High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection. Science 288 (2000) 1251-1253
27. Sanders L.H., Rockel A., Lu H., Wozniak D.J., and Sutton M.D. Role of the Pseudomonas aeruginosa dinB-encoded DNA polymerase IV in mutagenesis. J. Bacteriol. 188 (2006) 8573-8585
28. Mandsberg L.F., Ciofu O., Kirkby N., Christiansen L.E., Poulsen H.E., and Høiby N. Antibiotic resistance in P. aeruginosa with increased mutation frequency due to inactivation of the DNA oxidative repair system. Antimicrob. Agents Chemother. 53 (2009) 2483-2491
29. Morero N.R., and Argaraña C.E. Pseudomonas aeruginosa deficient in 8-oxodeoxyguanine repair system shows a high frequency of resistance to ciprofloxacin. FEMS Microbiol. Lett. 290 (2009) 217-226
30. Sanders L.H., Sudhakaran J., and Sutton M.D. The GO system prevents ROS-induced mutagenesis and killing in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 294 (2009) 89-96
31. Yee Y.C., Kisslinger B., Yu V.L., and Jin D.J. A mechanism of rifamycin inhibition and resistance in Pseudomonas aeruginosa. J. Antimicrob. Chemother. 38 (1996) 133-137
32. Hosokawa K., Park N.-H., Inaoka T., Itoh Y., and Ochi K. Streptomycin-resistant (rpsL) or rifampicin-resistant (rpoB) mutation in Pseudomonas putida KH146-2 confers enhanced resistance to organic chemicals. Environ. Microbiol. 4 (2002) 703-712
33. Meier P., and Wackernagel W. Impact of mutS inactivation on foreign DNA acquisition by natural transformation in Pseudomonas stutzeri. J. Bacteriol. 187 (2005) 143-154
34. Bayley S.A., Duggleby C.J., Worsey M.J., Williams P.A., Hardy K.G., and Broda P. Two modes of loss of the TOL function from Pseudomonas putida mt-2. Mol. Gen. Genet. 154 (1977) 203-204
35. Miller J.H. A Short Course in Bacterial Genetics (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
36. Adams M.H. Bacteriophages (1959), Interscience Publishers Inc., New York pp. 445-447
37. Lea D.E., and Coulson C.A. The distribution of the numbers of mutants in bacterial populations. J. Genet. 49 (1949) 264-265
38. Rosche W.A., and Foster P.L. Determining mutation rates in bacterial populations. Methods 20 (2000) 4-17
39. Musser J.M. Antimicrobial agent resistance in mycobacteria: molecular genetic insights. Clin. Microbial. Rev. 8 (1995) 496-514
40. Vogler A.J., Busch J.D., Percy-Fine S., Tipton-Hunton C., Smith K.L., and Keim P. Molecular analysis of rifampin resistance in Bacillus anthracis and Bacillus cereus. Antimicrob. Agents Chemother. 46 (2002) 511-513
41. Karunakaran P., and Davies J. Genetic antagonism and hypermutability in Mycobacterium smegmatis. J. Bacterial. 182 (2000) 3331-3335
42. Klein J.L., Brown T.J., and French G.L. Rifampin resistance in Mycobacterium kansasii is associated with rpoB mutations. Antimicrob. Agents Chemother. 45 (2001) 3056-3058
43. Cambau E., Bonnafous P., Perani E., Sougakoff W., Ji B., and Jarlier V. Molecular detection of rifampin and ofloxacin resistance for patients who experience relapse of multibacillary leprosy. Clin. Infect. Dis. 34 (2002) 39-45
44. Kim M., Wolff E., Huang T., Garibyan L., Earl A.M., Battista J.R., and Miller J.H. Developing a genetic system in Deinococcus radiodurans for analyzing mutations. Genetics 166 (2004) 661-668
45. Stefanelli P., Fazio C., La Rosa G., Marianelli C., Muscillo M., and Mastrantonio P. Rifampicin-resistant meningococci causing invasive disease: detection of point mutations in the rpoB gene and molecular characterization of the strains. J. Antimicrob. Chemother. 47 (2001) 219-222
46. Aubry-Damon H., Galimand M., gerbaud G., and Courvalin P. rpoB mutation conferring rifampin resistance in Streptococcus pyogenes. Antimicrob. Agents Chemother. 46 (2002) 1571-1573
47. Achour W., Guenni O., Fines M., Leclercq R., and Ben Hassen A. rpoB mutations in Streptococcus mitis clinical isolates resistant to rifampin. Antimicrob. Agents Chemother. 48 (2004) 2757-2759
48. Aubry-Damon H., Soussy C.-J., and Courvalin P. Characterization of mutations in the rpoB gene that confer rifampin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 42 (1998) 2590-2594
49. Fines M., Pronost S., Maillard K., Taouji S., and Leclercq R. Characterization of mutations in the rpoB gene associated with rifampin resistance in Rhodococcus equi isolated from foals. J. Clin. Microbiol. 39 (2001) 2784-2787
50. Heep M., Odenbreit S., Beck D., Decker J., Prohaska E., Rieger U., and Lehn N. Mutations at four distinct regions of the rpoB gene can reduce the susceptibility of Helicobacter pylori to rifamycins. Antimicrob. Agents Chemother. 44 (2000) 1713-1715
51. K. Nielsen, P. Hindersson, N. Høiby, M. Bangsborg, Sequencing of the rpoB gene in Legionella pneumophila and characterization of mutations associated with rifampin resistance in the legionellaceae, Antimicrob. Agents Chemother. 44 (2000) 2679-2683.
52. Schaaper R.M. Base selection, proofreading, and mismatch repair during DNA replication in Escherichia coli. J. Biol. Chem. 268 (1993) 23762-23765
53. Yazawa K., Mikami Y., Maeda A., Akao M., Morisaki N., and Iwasaki S. Inactivation of rifampin by Nocardia brasiliensis. Antimicrob. Agents Chemother. 37 (1993) 1313-1317
54. Dabbs E.R., Yazawa K., Mikami Y., Miyaji M., Morisaki N., Iwasaki S., and Furihata K. Ribosylation by mycobacterial strains as a new mechanism of rifampin inactivation. Antimicrob. Agents Chemother. 39 (1995) 1007-1009
55. Tanaka Y., Yazawa K., Dabbs E.R., Nishikawa K., Komaki H., Mikami Y., Miyaji M., Morisaki N., and Iwasaki S. Different rifampicin inactivation mechanisms in Nocardia and related taxa. Microbiol. Immunol. 40 (1996) 1-4
56. Quan S., Venter H., and Dabbs E.R. Ribosylative inactivation of rifampin by Mycobacterium smegmatis is a principal contributor to its low susceptibility to this antibiotic. Antimicrob. Agents Chemother. 41 (1997) 2456-2460
57. Hui J., Gordon N., and Kajioka R. Permeability barrier to rifampin in mycobacteria. Antimicrob. Agents Chemother. 11 (1997) 773-779
58. Chandrasekaran S., and Lalithakumari D. Plasmid-mediated rifampicin resistance in Pseudomonas fluorescens. J. Med. Microbiol. 47 (1998) 197-200
59. Schweizer H.P. Efflux as a mechanism of resistance to antimicrobials in Pseudomonas aeruginosa and related bacteria: unanswered questions. Genet. Mol. Res. 2 (2003) 46-62
60. Rossolini G.M., and Mantengoli E. Treatment and control of severe infections caused by multiresistant Pseudomonas aeruginosa. Clin. Microbial. Infect. 11 (2005) 17-32
61. Mesaros N., Glupczynski Y., Avrain L., Caceres N.E., Tulkens P.M., and Van Bambeke F. A combined phenotypic and genotypic method foe the detection of Mex efflux pumps in Pseudomonas aeruginosa. J. Antimicrob. Chemother. 59 (2007) 378-386
62. Lomovskaya O., Warren M.S., Lee A., Galazzo J., Fronko R., Lee M., Blais J., Cho D., Hamberland S., Renau T., Leger R., Hecker S., Watkins W., Hoshino K., Ishida H., and Lee V.J. Identification and characterization of inhibitors of multidrug resistance efflux pumps in Pseudomonas aeruginosa: novel agents for combination therapy. Antimicrob. Agents Chemother. 45 (2001) 105-116