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Nucleic Acids Research Advance Access originally published online on April 11, 2007
Nucleic Acids Research 2007 35(9):2861-2874; doi:10.1093/nar/gkm167
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Nucleic Acids Research, 2007, Vol. 35, No. 9 2861-2874
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

The domain structure of Helicobacter pylori DnaB helicase: the N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function

Ram Gopal Nitharwal1, Subhankar Paul2, Ashraf Dar1, Nirupam Roy Choudhury3, Rajesh K Soni1, Dhaneswar Prusty1, Sukrat Sinha1, Tara Kashav4, Gauranga Mukhopadhyay1, Tapan Kumar Chaudhuri2, Samudrala Gourinath4 and Suman Kumar Dhar1,*

1Special Centre for Molecular Medicine, Jawaharlal Nehru University, New Delhi 110067, India, 2Indian Institute of Technology, New Delhi, India, 3International Centre for Genetic Engineering and Biotechnology, New Delhi, India and 4School of Life Sciences, Jawaharlal Nehru University, New Delhi, India

*To whom correspondence should be addressed. Tel: +91-11-26704559; Fax: +91-11-26161781; Email: skdhar2002{at}yahoo.co.in

Received November 17, 2006. Revised February 25, 2007. Accepted March 4, 2007.

Hexameric DnaB type replicative helicases are essential for DNA strand unwinding along with the direction of replication fork movement. These helicases in general contain an amino terminal domain and a carboxy terminal domain separated by a linker region. Due to the lack of crystal structure of a full-length DnaB like helicase, the domain structure and function of these types of helicases are not clear. We have reported recently that Helicobacter pylori DnaB helicase is a replicative helicase in vitro and it can bypass Escherichia coli DnaC activity in vivo. Using biochemical, biophysical and genetic complementation assays, here we show that though the N-terminal region of HpDnaB is required for conformational changes between C6 and C3 rotational symmetry, it is not essential for in vitro helicase activity and in vivo function of the protein. Instead, an extreme carboxy terminal region and an adjacent unique 34 amino acid insertion region were found to be essential for HpDnaB activity suggesting that these regions are important for proper folding and oligomerization of this protein. These results confer great potential in understanding the domain structures of DnaB type helicases and their related function.


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