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PMID: 19729089 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Chapter 1: Variation in form and function the helix-turn-helix regulators of the GntR superfamily.

Advances in applied microbiology ·Vol. 69 ·2009-00-00 ·Pages 1-22

Hoskisson PA, Rigali S

Abstract

One of the most abundant and widely distributed groups of Helix-turn-helix (HTH) transcription factors is the metabolite-responsive GntR family of regulators (>8500 members in the Pfam database; Jan 2009). These proteins contain a DNA-binding HTH domain at the N terminus of the protein and an effector-binding and/or oligomerisation domain at the C terminus, where upon on binding an effector molecule, a conformational change occurs in the protein which influences the DNA-binding properties of the regulator resulting in repression or activation of transcription. This review summarises what we know about the distribution, structure, function and classification of these regulators and suggests that they may have a future role in biotechnology.

MeSH Terms
Amino Acid Sequence Anti-Bacterial Agents/biosynthesis Bacteria/genetics,metabolism,pathogenicity Bacterial Proteins/chemistry,genetics,metabolism Biotechnology DNA-Binding Proteins/chemistry,genetics,metabolism Evolution, Molecular Gene Expression Regulation, Bacterial Genes, Regulator Helix-Turn-Helix Motifs/genetics,physiology Molecular Sequence Data Protein Structure, Tertiary/genetics,physiology Sequence Alignment Virulence/genetics
Chemicals
Anti-Bacterial Agents Bacterial Proteins DNA-Binding Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hoskisson Paul A
Strathclyde Institute of Pharmacy and Biological Science, University of Strathclyde, Royal College Building, Glasgow, United Kingdom.
Rigali Sébastien
Article Info
Journal
Advances in applied microbiology
Abbr.
Adv Appl Microbiol
ISSN
0065-2164
Published
2009-00-00
Pages
1-22
Language
English
Region
United States
NLM ID
0370413
Subset
IM
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