ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Helicobacter pylori DprA alleviates restriction barrier for incoming DNA

Dwivedi, Gajendradhar R and Sharma, Eshita and Rao, Desirazu N (2013) Helicobacter pylori DprA alleviates restriction barrier for incoming DNA. In: Nucleic Acids Research, 41 (5). pp. 3274-3288.

[img] PDF
Nuc_Aci_Res_41-5_3274_2013.pdf - Published Version
Restricted to Registered users only

Download (713kB) | Request a copy
Official URL: http://dx.doi.org/10.1093/nar/gkt024

Abstract

Helicobacter pylori is a Gram-negative bacterium that colonizes human stomach and causes gastric inflammation. The species is naturally competent and displays remarkable diversity. The presence of a large number of restriction-modification (R-M) systems in this bacterium creates a barrier against natural transformation by foreign DNA. Yet, mechanisms that protect incoming double-stranded DNA (dsDNA) from restriction enzymes are not well understood. A DNA-binding protein, DNA Processing Protein A (DprA) has been shown to facilitate natural transformation of several Gram-positive and Gram-negative bacteria by protecting incoming single-stranded DNA (ssDNA) and promoting RecA loading on it. However, in this study, we report that H. pylori DprA (HpDprA) binds not only ssDNA but also dsDNA thereby conferring protection to both from various exo-nucleases and Type II restriction enzymes. Here, we observed a stimulatory role of HpDprA in DNA methylation through physical interaction with methyltransferases. Thus, HpDprA displayed dual functional interaction with H. pylori R-M systems by not only inhibiting the restriction enzymes but also stimulating methyltransferases. These results indicate that HpDprA could be one of the factors that modulate the R-M barrier during inter-strain natural transformation in H. pylori.

Item Type: Journal Article
Publication: Nucleic Acids Research
Publisher: Oxford University Press
Additional Information: Copyright of this article belongs to Oxford University Press.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 10 Jun 2013 07:47
Last Modified: 10 Jun 2013 07:47
URI: http://eprints.iisc.ac.in/id/eprint/46660

Actions (login required)

View Item View Item