Evaluation of DNA primase DnaG as a potential target for antibiotics

Antimicrobial Agents and Chemotherapy

Volumn 58, Issue 3, 2014, Pages 1699-1706

  Kuron, Aneta ^a   Korycka Machala, Malgorzata ^a   Brzostek, Anna ^a   Nowosielski, Marcin ^a   Doherty, Aidan ^b   Dziadek, Bozena ^c   Dziadek, Jaroslaw ^a  

^a INSTITUTE OF MEDICAL BIOLOGY   (Poland)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

^c UNIVERSITY OF LODZ   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

DNA PRIMASE; DNA PRIMASE DNAG; DOXORUBICIN; SURAMIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CHROMOSOME; BACTERIAL GROWTH; BACTERIAL SURVIVAL; BACTERIUM MUTANT; COMPUTER MODEL; CONTROLLED STUDY; DRUG TARGETING; ENZYME ACTIVITY; GENE DELETION; GENE INSERTION; HOMOLOGOUS RECOMBINATION; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN TARGETING; RNA SYNTHESIS; WILD TYPE;

ANTITUBERCULAR AGENTS; DNA PRIMASE; DOXORUBICIN; GENES, BACTERIAL; MICROBIAL SENSITIVITY TESTS; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; REAL-TIME POLYMERASE CHAIN REACTION; SURAMIN;

EID: 84896869208     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01721-13     Document Type: Article

References (41)

1. Dye C, Williams BG. 2010. The population dynamics and control of tuberculosis. Science 328:856-861. http://dx.doi.org/10.1126/science.1185449.
2. Gengenbacher M, Kaufmann SH. 2012. Mycobacterium tuberculosis: success through dormancy. FEMS Microbiol. Rev. 36:514-532. http://dx.doi.org/10.1111/j. 1574-6976.2012.00331.x.
3. Velayati AA, Masjedi MR, Farnia P, Tabarsi P, Ghanavi J, Ziazarifi AH, Hoffner SE. 2009. Emergence of new forms of totally drug-resistant tuberculosis bacilli: super extensively drug-resistant tuberculosis or totally drug-resistant strains in Iran. Chest 136:420-425. http://dx.doi.org/10.1378/chest.08-2427.
4. Centers for Disease Control and Prevention. 2006. Emergence of Mycobacterium tuberculosis with extensive resistance to second-line drugs worldwide, 2000-2004. MMWR Morb. Mortal. Wkly. Rep. 55:301-305.
5. Raviglione M. 2006. XDR-TB: entering the post-antibiotic era? Int. J. Tuberc. Lung Dis. 10:1185-1187. (Pubitemid 44713471)
6. Zhang Y, Vilcheze C, Jacobs WR, Jr. 2005. Mechanisms of drug resistance in Mycobacterium tuberculosis, p 115-142. In Cole ST, Eisenach KD, McMurray DN, Jacobs WR, Jr (ed), Tuberculosis and the tubercle bacillus. ASM Press, Washington, DC.
7. Griep MA. 1995. Primase structure and function. Indian J. Biochem. Biophys. 32:171-178.
8. Lao-Sirieix SH, Pellegrini L, Bell SD. 2005. The promiscuous primase. Trends Genet. 21:568-572. http://dx.doi.org/10.1016/j.tig.2005.07.010. (Pubitemid 41278462)
9. Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L. 2005. Structure of the heterodimeric core primase. Nat. Struct. Mol. Biol. 12: 1137-1144. http://dx.doi.org/10.1038/nsmb1013. (Pubitemid 41746786)
10. Corn JE, Berger JM. 2006. Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions. Nucleic Acids Res. 34:4082-4088. http://dx.doi.org/10.1093/nar/gkl363. (Pubitemid 44542187)
11. Iyer LM, Koonin EV, Leipe DD, Aravind L. 2005. Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members. Nucleic Acids Res. 33: 3875-3896. http://dx.doi.org/10.1093/nar/gki702. (Pubitemid 41418557)
12. Frick DN, Richardson CC. 2001. DNA primases. Annu. Rev. Biochem. 70:39-80. http://dx.doi.org/10.1146/annurev.biochem.70.1.39. (Pubitemid 32662205)
13. Weller GR, Doherty AJ. 2001. A family of DNA repair ligases in bacteria? FEBS Lett. 505:340-342. http://dx.doi.org/10.1016/S0014-5793(01)02831-9. (Pubitemid 32896692)
14. Aravind L, Koonin EV. 2001. Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system. Genome Res. 11:1365-1374. http://dx.doi.org/10.1101/gr.181001. (Pubitemid 32771543)
15. Pitcher RS, Tonkin LM, Green AJ, Doherty AJ. 2005. Domain structure of a NHEJ DNA repair ligase from Mycobacterium tuberculosis. J. Mol. Biol. 351:531-544. http://dx.doi.org/10.1016/j.jmb.2005.06.038. (Pubitemid 41021939)
16. Pitcher RS, Wilson TE, Doherty AJ. 2005. New insights into NHEJ repair processes in prokaryotes. Cell Cycle 4:675-678. http://dx.doi.org/10.4161/cc.4. 5.1676. (Pubitemid 41353850)
17. Weller GR, Kysela B, Roy R, Tonkin LM, Scanlan E, Della M, Devine SK, Day JP, Wilkinson A, d'Adda di Fagagna F, Devine KM, Bowater RP, Jeggo PA, Jackson SP, Doherty AJ. 2002. Identification of a DNA nonhomologous end-joining complex in bacteria. Science 297:1686-1689. http://dx.doi.org/10.1126/science.1074584. (Pubitemid 35000780)
18. Della M, Palmbos PL, Tseng HM, Tonkin LM, Daley JM, Topper LM, Pitcher RS, Tomkinson AE, Wilson TE, Doherty AJ. 2004. Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine. Science 306:683-685. http://dx.doi.org/10.1126/science.1099824. (Pubitemid 39440915)
19. Pitcher RS, Brissett NC, Picher AJ, Andrade P, Juarez R, Thompson D, Fox GC, Blanco L, Doherty AJ. 2007. Structure and function of a mycobacterial NHEJ DNA repair polymerase. J. Mol. Biol. 366:391-405. http://dx.doi.org/10.1016/j. jmb.2006.10.046. (Pubitemid 46136197)
20. Bartlett EJ, Brissett NC, Doherty AJ. 2013. Ribonucleolytic resection is required for repair of strand displaced nonhomologous end-joining intermediates. Proc. Natl. Acad. Sci. U. S. A. 110:E1984-E1991. http://dx.doi.org/10.1073/ pnas.1302616110.
21. Klann AG, Belanger AE, Abanes-De Mello A, Lee JY, Hatfull GF. 1998. Characterization of the dnaG locus in Mycobacterium smegmatis reveals linkage of DNA replication and cell division. J. Bacteriol. 180:65-72. (Pubitemid 28023784)
22. Snapper SB, Melton RE, Mustafa S, Kieser T, Jacobs WR, Jr. 1990. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4:1911-1919. http://dx.doi.org/10.1111/ j.1365-2958.1990.tb02040.x.
23. Sambrook J, Russell DW. 2001. Molecular cloning: a laboratory manual, 3rd ed, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
24. Parish T, Stoker NG. 2000. Use of a flexible cassette method to generate a double unmarked Mycobacterium tuberculosis tlyA plcABC mutant by gene replacement. Microbiology 146:1969-1975. (Pubitemid 30639272)
25. Brzostek A, Pawelczyk J, Rumijowska-Galewicz A, Dziadek B, Dziadek J. 2009. Mycobacterium tuberculosis is able to accumulate and utilize cholesterol. J. Bacteriol. 191:6584-6591. http://dx.doi.org/10.1128/JB.00488-09.
26. Pawelczyk J, Brzostek A, Kremer L, Dziadek B, Rumijowska-Galewicz A, Fiolka M, Dziadek J. 2011. AccD6, a key carboxyltransferase essential for mycolic acid synthesis in Mycobacterium tuberculosis, is dispensable in a nonpathogenic strain. J. Bacteriol. 193:6960-6972. http://dx.doi.org/10.1128/JB. 05638-11.
27. Swart JR, Griep MA. 1995. Primer synthesis kinetics by Escherichia coli primase on single-stranded DNA templates. Biochemistry 34:16097-16106. http://dx.doi.org/10.1021/bi00049a025.
28. Collins LA, Franzblau SG. 1997. Microplate Alamar Blue assay versus Bactec 460 system for high-throughput screening of compounds against Mycobacterium tuberculosis and Mycobacterium avium. Antimicrob. Agents Chemother. 41:1004 -1009.
29. Ciarrocchi G, MacPhee DG, Deady LW, Tilley L. 1999. Specific inhibition of the eubacterial DNA ligase by arylamino compounds. Antimicrob. Agents Chemother. 41:2766-2772. (Pubitemid 29519561)
30. Livak KJ, Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method. Methods 25: 402-408. http://dx.doi.org/10.1006/meth.2001.1262. (Pubitemid 34164012)
31. Kuchta RD, Stengel G. 2010. Mechanism and evolution of DNA primases. Biochim. Biophys. Acta 1804:1180-1189. http://dx.doi.org/10.1016/j.bbapap.2009. 06.011.
32. Biswas T, Resto-Roldán E, Sawyer SK, Artsimovitch I, Tsodikov OV. 2013. A novel non-radioactive primase-pyrophosphatase activity assay and its application to the discovery of inhibitors of Mycobacterium tuberculosis primase DnaG. Nucleic Acids Res. 41:e56. http://dx.doi.org/10.1093/nar/gks1292.
33. Chauhan A, Lofton H, Maloney E, Moore J, Fol M, Madiraju MV, Rajagopalan M. 2006. Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase. Mol. Microbiol. 62:132-147. http://dx.doi.org/10.1111/j. 1365-2958.2006.05333.x. (Pubitemid 44386555)
34. Korycka-Machala M, Rychta E, Brzostek A, Sayer HR, Rumijowska-Galewicz A, Bowater RP, Dziadek J. 2007. Evaluation of NAD(+)- dependent DNA ligase of mycobacteria as a potential target for antibiotics. Antimicrob. Agents Chemother. 51:2888-2897. http://dx.doi.org/10.1128/AAC.00254-07. (Pubitemid 47206227)
35. Srivastava SK, Tripathi RP, Ramachandran R. 2005. NAD+-dependent DNALigase (Rv3014c) from Mycobacterium tuberculosis. Crystal structure of the adenylation domain and identification of novel inhibitors. J. Biol. Chem. 280:30273-30281. http://dx.doi.org/10.1074/jbc.M503780200. (Pubitemid 41216207)
36. Dwivedi N, Dube D, Pandey J, Singh B, Kukshal V, Ramachandran R, Tripathi RP. 2008. NAD(+)-dependent DNA ligase: a novel target waiting for the right inhibitor. Med. Res. Rev. 28:545-568. http://dx.doi.org/10.1002/med.20114. (Pubitemid 351842142)
37. Trias J, Benz R. 1994. Permeability of the cell wall of Mycobacterium smegmatis. Mol. Microbiol. 14:283-290. http://dx.doi.org/10.1111/j.1365-2958. 1994.tb01289.x. (Pubitemid 24325805)
38. Draper P. 1998. The outer parts of the mycobacterial envelope as permeability barriers. Front. Biosci. 3:1253-1261.
39. Dziadek J, Rutherford SA, Madiraju MV, Atkinson MA, Rajagopalan M. 2003. Conditional expression of Mycobacterium smegmatis ftsZ, an essential cell division gene. Microbiology 149:1593-1603. http://dx.doi.org/10.1099/mic.0. 26023-0. (Pubitemid 36764082)
40. Lehman IR. 1974. DNA ligase: structure, mechanism, and function. Science 186:790-797. http://dx.doi.org/10.1126/science.186.4166.790.
41. Modrich P, Lehman IR. 1973. Deoxyribonucleic acid ligase. A steady state kinetic analysis of the reaction catalyzed by the enzyme from Escherichia coli. J. Biol. Chem. 248:7502-7511.