The C-terminal domain of DnaQ contains the polymerase binding site

Journal of Bacteriology

Volumn 181, Issue 9, 1999, Pages 2963-2965

  Taft Benz, Sharon A ^a   Schaaper, Roel M ^a  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE;

ARTICLE; BACTERIUM MUTANT; BINDING SITE; CHROMOSOME REPLICATION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; SITE DIRECTED MUTAGENESIS; YEAST;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 0032900274     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.9.2963-2965.1999     Document Type: Article

References (24)

1. Barnes, M. H., F. Spacciapoli, D. H. Li, and N. C. Brown. 1995. The 3′-5′ exonuclease site of DNA polymerase III from gram-positive bacteria: definition of a novel motif structure. Gene 165:45-50.
2. Bertram, J. G., L. B. Bloom, J. Turner, M. O'Donnell, J. M. Beechem, and M. F. Goodman. 1998. Pre-steady state analysis of the assembly of wild type and mutant circular clamps of Esckerichia coli DNA polymerase III onto DNA. J. Biol. Chem. 273:24564-24574.
3. Blanco, L., A. Bernad, and M. Salas. 1992. Evidence favouring the hypothesis of a conserved 3′-5′ exonuclease active site in DNA-dependent DNA polymerase. Gene 112:139-144.
4. Carter, J. R., M. A. Franden, R. Aebersold, D. R. Kim, and C. S. McHenry. 1993. Isolation, sequencing and overexpression of the gene encoding the θ subunit of DNA polymerase III holoenzyme. Nucleic Acids Res. 14:3281-3286.
5. Echols, H., C. Liu, and P. M. J. Burgers. 1983. Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme. Proc. Natl. Acad. Sci. USA 80:2189-2192.
6. Fijalkowska, I., and R. M. Schaaper. 1996. Mutants in the Exo I motif of Escherickia coli dnaQ: defective proofreading and inviability due to error catastrophe. Proc. Natl. Acad. Sci. USA 93:2856-2861.
7. Hingorani, M. M., and M. O'Donnell. 1998. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 273:24550-24563.
8. Jonczyk, P., A. Nowicka, I. J. Fijalkowska, R. M. Schaaper, and Z. Ciesla. 1998. In vivo protein interactions within the Escherichia coli DNA polymerase III core. J. Bacteriol. 180:1563-1566.
9. Kelman, Z., and M. O'Donnell. 1995. DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine. Annu. Rev. Biochem. 64:171-200.
10. Kornberg, A., and T. A. Baker. 1992. DNA replication. W. H. Freeman and Company, New York, N. Y.
11. Lancy, E. D., M. R. Lifsics, D. G. Kehres, and R. Maurer. 1989. Isolation and characterization of mutants with deletions in dnaQ, the gene for the editing subunit of DNA polymerase III of Salmonella typhimurium. J. Bacteriol. 171:5572-5580.
12. Lifsics, M. R., E. D. Lancy, Jr., and R. Maurer. 1992. DNA replication defect in Salmonella typhimurium mutants lacking the editing (ε) subunit of DNA polymerase III. J. Bacteriol. 174:6965-6973.
13. Link, A. J., D. Phillips, and G. M. Church. 1997. Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization. J. Bacteriol. 179:6228-6237.
14. Marians, K. J., H. Hiasa, D. R. Kim, and C. S. McHenry. 1998. Role of the core DNA polymerase III subunits at the replication fork. α is the only subunit required for processive replication. J. Biol. Chem. 273:2452-2457.
15. Maruyama, M., T. Horiuchi, H. Maki, and M. Sekiguchi. 1983. A dominant (mutD5) and a recessive (dnaQ49) mutator of Escherichia coli. J. Mol. Biol. 167:757-771.
16. McHenry, C. S. 1991. DNA polymerase III holoenzyme. Components, structure and mechanism of a true replicative complex. J. Biol. Chem. 266:19127-19130.
17. Perrino, F. W., S. Harvey, and S. M. McNeill. Personal communication.
18. Pham, P. T., M. W. Olson, C. S. McHenry, and R. M. Schaaper. 1998. The base substitution and frameshift fidelity of Escherichia coli DNA polymerase III holoenzyme in vitro. J. Biol. Chem. 273:23575-23584.
19. Rose, M. D., F. Winston, and P. Hieter. 1990. Methods in yeast genetics. A laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
20. Slater, S. C., M. R. Lifsics, M. O'Donnell, and R. Maurer. 1994. holE, the gene coding for the θ subunit of DNA polymerase III of Escherichia coli: characterization of a holE mutant and comparison with a dnaQ (ε-subunit) mutant. J. Bacteriol. 176:815-821.
21. Studwell-Vaughan, P. S., and M. O'Donnell. 1993. DNA polymerase III accessory proteins. V. θ encoded by holE. J. Biol. Chem. 268:11785-11791.
22. Sutrina, S. L., P. Reddy, M. H. Saier, Jr., and J. Reizer. 1990. The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease. J. Biol. Chem. 265:18581-18589.
23. Taft-Benz, S. A., and R. M. Schaaper. 1998. Mutational analysis of the 3′→5′ proofreading exonuclease of Escherichia coli DNA polymerase III. Nucleic Acids Res. 26:4005-4011.
24. Wootton, J. C., and M. H. Drummond. 1989. The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng. 2:535-543.