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PMID: 19633082 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri.

Journal of bacteriology ·Vol. 191 ·No. 22 ·2009-11-00 ·Pages 7121-2

Leduc JL, Roberts GP

Abstract

The protein Clp from Xanthomonas axonopodis pv. citri regulates pathogenesis and is a member of the CRP (cyclic AMP receptor protein) superfamily. We show that unlike the DNA-binding activity of other members of this family, the DNA-binding activity of Clp is allosterically inhibited by its effector and that cyclic di-GMP serves as that effector at physiological concentrations.

MeSH Terms

Allosteric Regulation/genetics,physiology Bacterial Proteins/genetics,metabolism Cyclic GMP/analogs & derivatives,metabolism,physiology DNA/metabolism Fluorescence Polarization Protein Binding Xanthomonas axonopodis/genetics,metabolism

Chemicals

Bacterial Proteins bis(3',5')-cyclic diguanylic acid DNA Cyclic GMP

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Leduc Jason L

Department of Bacteriology, 1550 Linden Drive, University of Wisconsin-Madison, Madison, WI 53706, USA.

Roberts Gary P

References (12)

12 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

1098-5530

DOI

10.1128/JB.00845-09

Published

2009-11-00

Epub

2009-00-24

Pages

7121-2

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC2772467

Subset

Grants

NIGMS NIH HHS · R01 GM053228 · United States

NIGMS NIH HHS · GM53228 · United States

Corrections

CommentIn

PMID: 19749051

External Links

PubMed source DOI: 10.1128/JB.00845-09 PMC Full Text View journal details

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Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri.

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