Bacterial replicases and related polymerases.

作者: Charles S McHenry

DOI: 10.1016/J.CBPA.2011.07.018

关键词:

摘要: Bacterial replicases are complex, tripartite replicative machines. They contain a polymerase, Pol III, β(2) processivity factor and DnaX complex ATPase that loads onto DNA chaperones III the newly loaded β(2). Many bacteria encode both full length τ shorter γ form of by variety mechanisms. The polymerase catalytic subunit α, contains PHP domain not only binds to prototypical ɛ Mg(2+)-dependent exonuclease, but also second Zn(2+)-dependent proofreading at least in some bacteria. Replication chromosomes low GC Gram-positive require two IIIs, one which, DnaE, appears extend RNA primers short distance before handing product off major replicase, PolC. Other (ImuC) apparently replaces V, required for induced mutagenesis E. coli. Approaches permit simultaneous biochemical screening all components bacterial promise inhibitors specific protein targets reaction stages.

参考文章(41)
Sho T. Yano, Lucia B. Rothman-Denes, A phage-encoded inhibitor of Escherichia coli DNA replication targets the DNA polymerase clamp loader Molecular Microbiology. ,vol. 79, pp. 1325- 1338 ,(2011) , 10.1111/J.1365-2958.2010.07526.X
Arthur E Pritchard, H Garry Dallmann, Bradley P Glover, Charles S McHenry, A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of δδ′ with DnaX4 forms DnaX3δδ′ The EMBO Journal. ,vol. 19, pp. 6536- 6545 ,(2000) , 10.1093/EMBOJ/19.23.6536
Meindert H. Lamers, Roxana E. Georgescu, Sang-Gyu Lee, Mike O'Donnell, John Kuriyan, Crystal Structure of the Catalytic α Subunit of E. coli Replicative DNA Polymerase III Cell. ,vol. 126, pp. 881- 892 ,(2006) , 10.1016/J.CELL.2006.07.028
Errol C. Friedberg, Alan R. Lehmann, Robert P.P. Fuchs, Trading places: how do DNA polymerases switch during translesion DNA synthesis? Molecular Cell. ,vol. 18, pp. 499- 505 ,(2005) , 10.1016/J.MOLCEL.2005.03.032
Audrey Costes, François Lecointe, Stephen McGovern, Sophie Quevillon-Cheruel, Patrice Polard, The C-Terminal Domain of the Bacterial SSB Protein Acts as a DNA Maintenance Hub at Active Chromosome Replication Forks PLoS Genetics. ,vol. 6, pp. e1001238- 15 ,(2010) , 10.1371/JOURNAL.PGEN.1001238
R. Reyes-Lamothe, D. J. Sherratt, M. C. Leake, Stoichiometry and architecture of active DNA replication machinery in Escherichia coli. Science. ,vol. 328, pp. 498- 501 ,(2010) , 10.1126/SCIENCE.1185757
Anna Wieczorek, Christopher D. Downey, H. Garry Dallmann, Charles S. McHenry, Only One ATP-binding DnaX Subunit Is Required for Initiation Complex Formation by theEscherichia coliDNA Polymerase III Holoenzyme Journal of Biological Chemistry. ,vol. 285, pp. 29049- 29053 ,(2010) , 10.1074/JBC.C110.165076
Charles S McHenry, Breaking the rules: bacteria that use several DNA polymerase IIIs EMBO Reports. ,vol. 12, pp. 408- 414 ,(2011) , 10.1038/EMBOR.2011.51
Rodrigo S Galhardo, Raquel P Rocha, Marilis V Marques, Carlos FM Menck, None, An SOS-regulated operon involved in damage-inducible mutagenesis in Caulobacter crescentus. Nucleic Acids Research. ,vol. 33, pp. 2603- 2614 ,(2005) , 10.1093/NAR/GKI551
Peter McInerney, Aaron Johnson, Francine Katz, Mike O'Donnell, Characterization of a Triple DNA Polymerase Replisome Molecular Cell. ,vol. 27, pp. 527- 538 ,(2007) , 10.1016/J.MOLCEL.2007.06.019