Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 19 October 2007:
Vol. 318. no. 5849, pp. 459 - 463
DOI: 10.1126/science.1147353
Prev | Table of Contents | Next

Reports

Structure of Hexameric DnaB Helicase and Its Complex with a Domain of DnaG Primase

Scott Bailey,1 William K. Eliason,1 Thomas A. Steitz1,2*

The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.

1 Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.
2 Department of Chemistry, Yale University, New Haven, CT 06520, USA.

* To whom correspondence should be addressed. E-mail: eatherton{at}csb.yale.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A biochemically active MCM-like helicase in Bacillus cereus.
M. Samuels, G. Gulati, J.-H. Shin, R. Opara, E. McSweeney, M. Sekedat, S. Long, Z. Kelman, and D. Jeruzalmi (2009)
Nucleic Acids Res.
   Abstract »    Full Text »    PDF »
A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader.
K. V. Loscha, K. Jaudzems, C. Ioannou, X.-C. Su, F. R. Hill, G. Otting, N. E. Dixon, and E. Liepinsh (2009)
Nucleic Acids Res. 37, 2395-2404
   Abstract »    Full Text »    PDF »
The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA.
Y.-H. Lo, K.-L. Tsai, Y.-J. Sun, W.-T. Chen, C.-Y. Huang, and C.-D. Hsiao (2009)
Nucleic Acids Res. 37, 804-814
   Abstract »    Full Text »    PDF »
Mcm Subunits Can Assemble into Two Different Active Unwinding Complexes.
D. M. Kanter, I. Bruck, and D. L. Kaplan (2008)
J. Biol. Chem. 283, 31172-31182
   Abstract »    Full Text »    PDF »
Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity.
G. T. Haugland, N. Sakakibara, A. L. Pey, C. R. Rollor, N.-K. Birkeland, and Z. Kelman (2008)
Nucleic Acids Res. 36, 5602-5609
   Abstract »    Full Text »    PDF »
Physiological and Biochemical Defects in Carboxyl-terminal Mutants of Mitochondrial DNA Helicase.
Y. Matsushima, C. L. Farr, L. Fan, and L. S. Kaguni (2008)
J. Biol. Chem. 283, 23964-23971
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)