Literature DB >> 10095066

The Bacillus stearothermophilus replicative helicase: cloning, overexpression and activity.

L E Bird1, D B Wigley.   

Abstract

As part of biochemical and structural studies of the primosome of a gram positive bacterial species, we describe the cloning of the Bacillus stearothermophilus replicative helicase, DnaB. The protein is 45% and 82% identical to the Escherichia coli and B. subtilis replicative helicases, respectively. Recombinant DnaB was purified and shown to be an active helicase.

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Year:  1999        PMID： 10095066     DOI： 10.1016/s0167-4781(99)00024-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  11 in total

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

Authors:  P Soultanas; D B Wigley
Journal:  Nucleic Acids Res       Date:  2002-09-15       Impact factor: 16.971

2.  Class-specific restrictions define primase interactions with DNA template and replicative helicase.

Authors:  Marilynn A Larson; Mark A Griep; Rafael Bressani; Kiran Chintakayala; Panos Soultanas; Steven H Hinrichs
Journal:  Nucleic Acids Res       Date:  2010-06-30       Impact factor: 16.971

3.  Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.

Authors:  Kiran Chintakayala; Cristina Machón; Anna Haroniti; Marilyn A Larson; Steven H Hinrichs; Mark A Griep; Panos Soultanas
Journal:  Mol Microbiol       Date:  2009-04       Impact factor: 3.501

4.  Functional characterization of Helicobacter pylori DnaB helicase.

Authors:  Rajesh K Soni; Parul Mehra; Nirupam Roy Choudhury; Gauranga Mukhopadhyay; Suman Kumar Dhar
Journal:  Nucleic Acids Res       Date:  2003-12-01       Impact factor: 16.971

5.  Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus.

Authors:  L E Bird; H Pan; P Soultanas; D B Wigley
Journal:  Biochemistry       Date:  2000-01-11       Impact factor: 3.162

6.  DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings.

Authors:  Jenny Thirlway; Ian J Turner; Christopher T Gibson; Laurence Gardiner; Kevin Brady; Stephanie Allen; Clive J Roberts; Panos Soultanas
Journal:  Nucleic Acids Res       Date:  2004-06-01       Impact factor: 16.971

7.  A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus.

Authors:  P Soultanas
Journal:  Nucleic Acids Res       Date:  2002-02-15       Impact factor: 16.971

8.  Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein.

Authors:  A Haroniti; R Till; M C M Smith; P Soultanas
Journal:  Biochemistry       Date:  2003-09-23       Impact factor: 3.162

9.  Domain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues.

Authors:  Kiran Chintakayala; Marilynn A Larson; William H Grainger; David J Scott; Mark A Griep; Steven H Hinrichs; Panos Soultanas
Journal:  Mol Microbiol       Date:  2007-03       Impact factor: 3.501

10.  Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase.

Authors:  José P Afonso; Kiran Chintakayala; Chatrudee Suwannachart; Svetlana Sedelnikova; Kevin Giles; John B Hoyes; Panos Soultanas; John B Rafferty; Neil J Oldham
Journal:  Nucleic Acids Res       Date:  2013-03-21       Impact factor: 16.971
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