Strathprints Home | Open Access | Browse | Search | User area | Copyright | Help | Library Home | SUPrimo

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

Hoskisson, P. and Rigali, S. (2009) Variation in form and function: the helix-turn-helix regulators of the GntR superfamily. In: Advances in Applied Microbiology. Advances in Applied Microbiology, 69 . Elsevier, pp. 1-22. ISBN 9780123748249

Full text not available in this repository. (Request a copy from the Strathclyde author)

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.

Item type: Book Section
ID code: 25963
Keywords: GntR, helix-turn-helix, repressor protein, dna binding, autoregulation, streptomyces, Chemical technology, Genetics, Microbiology
Subjects: Technology > Chemical technology
Science > Natural history > Genetics
Science > Microbiology
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Related URLs:
    Depositing user: Strathprints Administrator
    Date Deposited: 26 Aug 2010 10:18
    Last modified: 12 Mar 2012 11:15
    URI: http://strathprints.strath.ac.uk/id/eprint/25963

    Actions (login required)

    View Item