Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus

Nucleic Acids Research

Volumn 30, Issue 18, 2002, Pages 4051-4060

  Soultanas, P ^a   Wigley, D B ^b  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^b IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA B; DNA PRIMASE; GLUTAMIC ACID; HELICASE; MAGNESIUM ION; NUCLEOTIDE; PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; DNA BINDING MOTIF; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENETIC CONSERVATION; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS;

BACILLUS STEAROTHERMOPHILUS; BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS; POSIBACTERIA;

EID: 0037106446     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkf527     Document Type: Article

References (40)

1. LeBowitz,J.H. and McMacken,R. (1986). The Escherichia coli dnaB replication protein is a DNA helicase. J. Biol. Chem, 261, 4738-4748.
2. Reha-Krantz,L.J, and Hurwitz,J. (1978) The dnaB gene product of Escherichia coli. I. Purification, homogeneity and physical properties. J. Biol. Chem., 253, 4043-4050.
3. Bujalowski,W., KlonowskaM.M. and Jezewska,M,J, (1994) Oligomeric structure of Eschericia coli primary replicative helicase DnaB protein. J. Biol. Chem. 269, 31350-31358.
4. Bird,L.E., Hu,P., Soultanas,P. and Wigley,D.B. (2000) Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry, 39, 171-182.
5. Biswas,E.E. and Biswas,S.B. (1999) Mechanism of DnaB helicase of Escherichia coli: structural domains involved in ATP hydrolysis, DNA binding and oligomerization, Biochemistry, 38, 10919-10928.
6. Marszalek,J. and Kaguni,J.M. (1994) DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli. J. Biol. Chem. 269, 4883-4890.
7. Wickner,S. and Hurwitz,J. (1975) Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro. Proc. Natl Acad. Sci. USA, 72, 921-925.
8. Soultanas,P. (2002) A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus. Nucleic Acids Res., 30, 966-974.
9. Tougu,K. and Marians,K.J. (1996) The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J. Biol. Chem. 271, 21391-21397.
10. Tougu,K. and Marians,K.J. (1996) The interaction between helicase and primase sets the replication fork clock. J. Biol. Chem. 271, 21398-21405.
11. Kornberg,A. and Baker,T.A. (1992) DNA Replication, 2nd Edn. W.H.Freeman and Co., San Francisco, CA.
12. Tougu,K., Peng,H. and Marians,K.J. (1994) Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem., 269, 46765-4682.
13. Kobori,J.A. and Kornberg,A. (1982) The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex. J. Biol. Chem., 257, 13770-13775.
14. Wahle,E., Lasken,R.S. and Kornberg,A. (1989) The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions. J. Biol. Chem., 264, 2469-2475.
15. Funnell,B.E., Baker,T.A. and Kornberg,A. (1987) In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. J. Biol. Chem. 262, 10327-1033.
16. Mllory,J.B., Alfano,C. and McMaken,R. (1990) Host virus interactions in the initiation of bactriophage lambda DNA replication. Recruitment of Echerichia coli DnaB helicase by lambda P replication protein. J. Biol. Chem. 265, 13297-13307.
17. Liberek,K. Georgopoulos,C. and Zylicz,M. (1988) Role of the Escherichia coli DnaK and DnaJ heat shock protein in the initiation of bactriophage lambda DNA replication. Proc. Natl Acad. Sci. USA, 85, 5532-6636.
18. Marians,K.J. (1992) Prokaryotic DNA replication. Annu. Rev. Biochem., 61, 673-719.
19. Chang,P. and Marians,K.J. (2002) Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork. J. Biol. Chem. 275, 26187-26195.
20. McPherson,M.J., Quirke,P. and Taylor,G.R. (1992) PCR: A Practical Approach. IRL Press, Oxford, UK, pp. 207-209.
21. Soultanas,P., Dillingham,M.S. Velankar,S.S. and Wigley,D.B. (1999) DNA binding mediates conformation changs and metal ion coordination in the active site of PcrA helicase. J. Mol. Biol., 290, 137-148.
22. Bird,L.E. and Wigley,D.B. (1999) The Bacillus stearothermophilus replicative helicase: cloning, overexpression and activity. Biochim. Biophys. Acta, 1444, 424-428.
23. Laemmli,U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
24. Pullman,M.E., Penefsky,H.S., Datta,A. and Racker,E. (1960) Partial resolution of the enzymes catalysing oxidative phosphorylation. J. Biol. Chem. 235, 3322-3329.
25. Soultanas,P., Dillingham,M.S., Papadopoulos,F., Phillips,S.E.V., Thomas,C.D. and Wigley, D.B. (1999) Plasmid replication initiator protein RepD increases the processitivity of PcrA DNA helicase. Nucleic Acids Res., 27, 1421-1428.
26. Walker,J.E., Saraste,M. Runswick,M.J. and Gray,N.J. (1982) Distantly related sequences in the alpha- and beta-subnits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J., 1, 945-951.
27. Sawaya,M.R. Guo,S., Tabor,S., Richardson,C.C. and Ellenberger,T. (1999) Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell, 99, 167-177
28. Singleton,M.R., Sawaya,M.R., Ellenberger,T. and Wigley,D.B. (2000) Crystal structure of T7 gene 4 ring helicase indicated a mechanism for sequential hydrolysis of nucleotides. Cell, 101, 589-600.
29. Neidenzu,T., Roleke,D., Bains,G., Scherzinger,E. and Sanger,W. (2001) Crystal structure of the hexameric replicative helicase RepA of plasmid RSF1010. J. Mol. Biol., 306, 479-487.
30. Subramanya,H.S., Bird,L.E., Branningan,J.A. and Wigley,D.B. (1996) Crystal structure of a DExx box DNA helicase. Nature, 384, 379-383.
31. Story,R.M. and Steitz,T.A. (1992) Structure of the recA protein-ADP complex. Nature, 355, 374-376.
32. Velankar,S.S., Soultanas,P., Dillingham,M.S., Subramanya,H.S. and Wigley,D.B. (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell, 97, 75-84.
33. Kelley,J.A. and Knight,K.L. (1997) Allosteric regulation of RecA protein function is mediated by Gln194. J. Biol. Chem., 272, 25778-25782.
34. Washington,M.T., Rosenberg,A.H., Griffin,K., Studier,F.W. and Patel,S.S. (1996) Biochemical analysis of mutant hydrolysis and the proteins defective in DNA binding, nucleotide hydrolysis and the coupling of hydrolysis with DNA unwinding. J. Biol. Chem., 271, 26825-26834.
35. Patel,S.S., Hingorani,M.M. and Ng,W.M. (1994) The K318A mutant of bacteriophage T7 DNA primase-helicase protein wild-type but not primase activity and inhibits primase-helicase protein wild-type activities by heterooligomer formation. Biochemistry, 33, 7857-7868.
36. Korolev,S., Hsieh,J., Gauss,G.H., Lohman,T.M. and Walksman,G. (1997) Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell, 90, 635-647.
37. Cho,H.S., Ha,N.C., Kang,L.W., Chung,K.M., Back,S.H., Jang,S.K. and Oh,B.H. (1998) Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanisms of unwinding duplex RNA. J. Biol. Chem., 273, 15045-15052.
38. Dillingham,M.S., Soultanas,P. and Wigley,D.B. (1999) Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation. Nucleic Acids Res., 27, 3310-3317.
39. Hingorani,M.M. and Patel,S.S. (1993) Interaction of bacteriophage T7 DNA primase/helicae protein with single-stranded and double-stranded DNAs. Biochemistry, 32, 12478-12487.
40. 2+. The presence of dTTP is sufficient for hexamer formation and DNA binding. J. Biol. Chem., 273, 27315-27319.