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Insights into the Functional Roles of N-Terminal and C-Terminal Domains of Helicobacter pylori DprA

Dwivedi, Gajendradhar R and Srikanth, Kolluru D and Anand, Praveen and Naikoo, Javed and Srilatha, NS and Rao, Desirazu N (2015) Insights into the Functional Roles of N-Terminal and C-Terminal Domains of Helicobacter pylori DprA. In: PLOS ONE, 10 (7).

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Official URL: http://dx.doi.org/10.1371/journal.pone.0131116


DNA processing protein A (DprA) plays a crucial role in the process of natural transformation. This is accomplished through binding and subsequent protection of incoming foreign DNA during the process of internalization. DprA along with Single stranded DNA binding protein A (SsbA) acts as an accessory factor for RecA mediated DNA strand exchange. H. pylori DprA (HpDprA) is divided into an N-terminal domain and a C-terminal domain. In the present study, individual domains of HpDprA have been characterized for their ability to bind single stranded (ssDNA) and double stranded DNA (dsDNA). Oligomeric studies revealed that HpDprA possesses two sites for dimerization which enables HpDprA to form large and tightly packed complexes with ss and dsDNA. While the N-terminal domain was found to be sufficient for binding with ss or ds DNA, C-terminal domain has an important role in the assembly of poly-nucleoprotein complex. Using site directed mutagenesis approach, we show that a pocket comprising positively charged amino acids in the N-terminal domain has an important role in the binding of ss and dsDNA. Together, a functional cross talk between the two domains of HpDprA facilitating the binding and formation of higher order complex with DNA is discussed.

Item Type: Journal Article
Publication: PLOS ONE
Additional Information: Copy right for this article belongs to the PUBLIC LIBRARY SCIENCE, 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 19 Aug 2015 05:58
Last Modified: 19 Aug 2015 05:58
URI: http://eprints.iisc.ac.in/id/eprint/52148

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