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| Content Provider | PubMed Central |
|---|---|
| Author | Marston, Farhat Y. Grainger, William H. Smits, Wiep Klaas Hopcroft, Nicholas H. Green, Matthew Hounslow, Andrea M. Grossman, Alan D. Craven, C. Jeremy Panos, Soultanas |
| Copyright Year | 2010 |
| Abstract | DnaD and DnaB are essential DNA-replication-initiation proteins in low-G+C content Gram-positive bacteria. Here we use sensitive Hidden Markov Model-based techniques to show that the DnaB and DnaD proteins share a common structure that is evident across all their structural domains, termed DDBH1 and DDBH2 (DnaD DnaB Homology 1 and 2). Despite strong sequence divergence, many of the DNA-binding and oligomerization properties of these domains have been conserved. Although eluding simple sequence comparisons, the DDBH2 domains share the only strong sequence motif; an extremely highly conserved YxxxIxxxW sequence that contributes to DNA binding. Sequence alignments of DnaD alone fail to identify another key part of the DNA-binding module, since it includes a poorly conserved sequence, a solvent-exposed and somewhat unstable helix and a mobile segment. We show by NMR, in vitro mutagenesis and in vivo complementation experiments that the DNA-binding module of Bacillus subtilis DnaD comprises the YxxxIxxxW motif, the unstable helix and a portion of the mobile region, the latter two being essential for viability. These structural insights lead us to a re-evaluation of the oligomerization and DNA-binding properties of the DnaD and DnaB proteins. |
| Related Links | http://dx.doi.org/10.1093/nar/gkq465 |
| Starting Page | 6930 |
| File Format | |
| ISSN | 13624962 |
| e-ISSN | 13624962 |
| Journal | Nucleic Acids Research |
| Issue Number | 20 |
| Volume Number | 38 |
| Language | English |
| Publisher | Oxford University Press |
| Publisher Date | 2010-11-01 |
| Access Restriction | Open |
| Rights Holder | Oxford University Press |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics |
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