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Helicobacter pylori single-stranded DNA binding protein--functional characterization and modulation of H. pylori DnaB helicase activity.
FEBS J. 2009 Jan; 276(2):519-31
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14 Jan 2009
Interesting Hypothesis, New Finding
DOI: 10.3410/f.1146839.603924
DNA replication is an important cellular process in bacteria, which is perhaps not much favoured during dormancy. Various DNA-binding proteins have critical roles in achieving a check on replication, so long as the environment is not favourable for active growth. Suman Dhar and colleagues used Helicobacter...Continue reading
DNA replication is an important cellular process in bacteria, which is perhaps not much favoured during dormancy. Various DNA-binding proteins have critical roles in achieving a check on replication, so long as the environment is not favourable for active growth. Suman Dhar and colleagues used Helicobacter pylori coccoid versus vegetative lifestyle as a model to investigate the basics of stress response of the bacterium at the interface of an important metabolic process such as replication.
Using in vitro expressed and purified proteins SSB and DnaB, the authors demonstrated that coccoid forms of H. pylori, as compared to their vegetative forms, do not orchestrate formation of active replication forks, thus preventing active replication and thereby growth.
The authors, for the first time, provide a meaningful insight into H. pylori replication at the molecular level. They also delineate the role of various DNA-binding proteins in the replication check mechanism, as well as the replication process itself.
Using in vitro expressed and purified proteins SSB and DnaB, the authors demonstrated that coccoid forms of H. pylori, as compared to their vegetative forms, do not orchestrate formation of active replication forks, thus preventing active replication and thereby growth.
The authors, for the first time, provide a meaningful insight into H. pylori replication at the molecular level. They also delineate the role of various DNA-binding proteins in the replication check mechanism, as well as the replication process itself.
Disclosures
None declared
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Ahmed N: F1000Prime Recommendation of [Sharma A et al., FEBS J 2009, 276(2):519-31]. In F1000Prime, 14 Jan 2009; DOI: 10.3410/f.1146839.603924. F1000Prime.com/1146839#eval603924
F1000Prime Recommendations, Dissents and Comments for [Sharma A et al., FEBS J 2009, 276(2):519-31]. In F1000Prime, 19 May 2013; F1000Prime.com/1146839
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Helicobacter pylori, an important bacterial pathogen, causes gastric ulcer and gastric adenocarcinoma in humans. The fundamentals of basic biology such as DNA replication are poorly understood in this pathogen. In the present study, we report the cloning and functional characterization of the single-stranded DNA (ssDNA) binding protein from H. pylori. The N-terminal DNA binding domain shows significant homology with E. coli single-stranded DNA binding protein (SSB), whereas the C-terminal domain shows less homology. The overall DNA-binding activity and tetramerization properties, however, remain unaffected. In in vitro experiments with purified proteins, H. pylori (Hp) SSB bound specifically to ssDNA and modulated the enzymatic ATPase and helicase activity of HpDnaB helicase. HpSSB and HpDnaB proteins were co-localized in sharp, distinct foci in exponentially growing H. pylori cells, whereas both were spread over large areas in its dormant coccoid form, suggesting the absence of active replication forks in the latter. These results confirm the multiple roles of SSB during DNA replication and provide evidence for altered replicative metabolism in the spiral and coccoid forms that may be central to the bacterial physiology and pathogenesis.
DOI: 10.1111/j.1742-4658.2008.06799.x
PMID: 19087193
