Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (233K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Rousseau, P.
Right arrow Articles by Chandler, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rousseau, P.
Right arrow Articles by Chandler, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 23 February 2004

Nucleic Acids Research, 2004, Vol. 32, No. 4 1335-1344
© 2004 Oxford University Press

The helix–turn–helix motif of bacterial insertion sequence IS911 transposase is required for DNA binding

Philippe Rousseau*, Erwan Gueguen, Guy Duval-Valentin and Mick Chandler

Laboratoire de Microbiologie et de Génétique Moléculaire, CNRS, 118 Route de Narbonne, F-31062 Toulouse Cedex, France

*To whom correspondence should be addressed. Tel: +33 5 61 33 59 16; Fax: +33 5 61 33 58 86; Email: philippe.rousseau{at}ibcg.biotoul.fr

The transposase of IS911, a member of the IS3 family of bacterial insertion sequences, is composed of a catalytic domain located at its C-terminal end and a DNA binding domain located at its N-terminal end. Analysis of the transposases of over 60 members of the IS3 family revealed the presence of a helix–turn–helix (HTH) motif within the N-terminal region. Alignment of these potential secondary structures further revealed a completely conserved tryptophan residue similar to that found in the HTH motifs of certain homeodomain proteins. The analysis also uncovered a similarity between the IS3 family HTH and that of members of the LysR family of bacterial transcription factors. This information was used to design site-directed mutations permitting an assessment of its role in transposase function. A series of in vivo and in vitro tests demonstrated that the HTH domain is important in directing the transposase to bind the terminal inverted repeats of IS911.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Microbiol. Mol. Biol. Rev.Home page
J. L. Ramos, M. Martinez-Bueno, A. J. Molina-Henares, W. Teran, K. Watanabe, X. Zhang, M. T. Gallegos, R. Brennan, and R. Tobes
The TetR Family of Transcriptional Repressors
Microbiol. Mol. Biol. Rev., June 1, 2005; 69(2): 326 - 356.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.