umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
pH-dependent conformational switch activates the inhibitor of transcription elongation
Department of Cell Biology, School of Osteopathic Medicine at Stratford, University of Medicine and Dentistry of New Jersey, Stratford, NJ, USA.
Department of Biochemistry, New York University School of Medicine, New York, NY, USA.
Department of Cell Biology, School of Osteopathic Medicine at Stratford, University of Medicine and Dentistry of New Jersey, Stratford, NJ, USA.
Department of Cell Biology, School of Osteopathic Medicine at Stratford, University of Medicine and Dentistry of New Jersey, Stratford, NJ, USA.
Show others and affiliations
2006 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 25, no 10, 2131-2141 p.Article in journal (Refereed) Published
Abstract [en]

Gfh1, a transcription factor from Thermus thermophilus, inhibits all catalytic activities of RNA polymerase (RNAP). We characterized the Gfh1 structure, function and possible mechanism of action and regulation. Gfh1 inhibits RNAP by competing with NTPs for coordinating the active site Mg2+ ion. This coordination requires at least two aspartates at the tip of the Gfh1 N-terminal coiled-coil domain (NTD). The overall structure of Gfh1 is similar to that of the Escherichia coli transcript cleavage factor GreA, except for the flipped orientation of the C-terminal domain (CTD). We show that depending on pH, Gfh1-CTD exists in two alternative orientations. At pH above 7, it assumes an inactive 'flipped' orientation seen in the structure, which prevents Gfh1 from binding to RNAP. At lower pH, Gfh1-CTD switches to an active 'Gre-like' orientation, which enables Gfh1 to bind to and inhibit RNAP.

Place, publisher, year, edition, pages
2006. Vol. 25, no 10, 2131-2141 p.
Keyword [en]
active center, inhibitor, RNA polymerase, transcription elongation factors, transcription regulation
National Category
Biochemistry and Molecular Biology Cell Biology
Identifiers
URN: urn:nbn:se:umu:diva-81881DOI: 10.1038/sj.emboj.7601094ISI: 000237590000009PubMedID: 16628221OAI: oai:DiVA.org:umu-81881DiVA: diva2:658619
Available from: 2013-10-22 Created: 2013-10-22 Last updated: 2017-12-06Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

Cava, Felipe

Search in DiVA

By author/editor
Cava, Felipe
In the same journal
EMBO Journal
Biochemistry and Molecular BiologyCell Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 39 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf