Skip Navigation



Nucleic Acids Research Advance Access published online on November 6, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn827
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (9798K) Freely available
Right arrow Screen PDF (1739K) Freely available
Right arrowOA All Versions of this Article:
36/22/7110    most recent
gkn827v1
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 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 Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Gao, Y.-G.
Right arrow Articles by Yao, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gao, Y.-G.
Right arrow Articles by Yao, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 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.

Structural Biology

Structural and functional characterization of the LldR from Corynebacterium glutamicum: a transcriptional repressor involved in L-lactate and sugar utilization

Yong-Gui Gao1, Hiroaki Suzuki2, Hiroshi Itou3, Yong Zhou1, Yoshikazu Tanaka1, Masaaki Wachi2, Nobuhisa Watanabe1, Isao Tanaka1 and Min Yao1,*

1Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, 2Department of Bioengineering, Tokyo Institute of Technology, Yokohama 226-8503 and 3National Institute of Genetics, Mishima, Shizuoka 411-8540, Japan

*To whom correspondence should be addressed. Tel: +81 11 706 4481; Fax: +81 11 706 4481; Email: yao{at}castor.sci.hokudai.ac.jp

Received July 4, 2008. Revised October 9, 2008. Accepted October 14, 2008.

LldR (CGL2915) from Corynebacterium glutamicum is a transcription factor belonging to the GntR family, which is typically involved in the regulation of oxidized substrates associated with amino acid metabolism. In the present study, the crystal structure of LldR was determined at 2.05-Å resolution. The structure consists of N- and C-domains similar to those of FadR, but with distinct domain orientations. LldR and FadR dimers achieve similar structures by domain swapping, which was first observed in dimeric assembly of transcription factors. A structural feature of Zn2+ binding in the regulatory domain was also observed, as a difference from the FadR subfamily. DNA microarray and DNase I footprint analyses suggested that LldR acts as a repressor regulating cgl2917-lldD and cgl1934-fruK-ptsF operons, which are indispensable for L-lactate and fructose/sucrose utilization, respectively. Furthermore, the stoichiometries and affinities of LldR and DNAs were determined by isothermal titration calorimetry measurements. The transcriptional start site and repression of LldR on the cgl2917-lldD operon were analysed by primer extension assay. Mutation experiments showed that residues Lys4, Arg32, Arg42 and Gly63 are crucial for DNA binding. The location of the putative ligand binding cavity and the regulatory mechanism of LldR on its affinity for DNA were proposed.

Present address: Yong-Gui Gao, MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK


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
 J. Bacteriol.Home page
K. Toyoda, H. Teramoto, M. Inui, and H. Yukawa
The ldhA Gene, Encoding Fermentative L-Lactate Dehydrogenase of Corynebacterium glutamicum, Is under the Control of Positive Feedback Regulation Mediated by LldR
J. Bacteriol., July 1, 2009; 191(13): 4251 - 4258.
[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.