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
The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain
Department of Biology, University of Copenhagen, Centre for Bacterial Stress Response and Persistence, Copenhagen 2200, Denmark; Present address: Department of Molecular Biology, Umeå University, 901 87 Umeå , Sweden.
Show others and affiliations
2019 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 27, no 11, p. 1675-+Article in journal (Refereed) Published
Abstract [en]

The E. coli hicAB type II toxin-antitoxin locus is unusual by being controlled by two promoters and by having the toxin encoded upstream of the antitoxin. HicA toxins contain a double-stranded RNA-binding fold and cleaves both mRNA and tmRNA in vivo, while HicB antitoxins contain a partial RNase H fold and either a helix-turn-helix (HTH) or ribbon-helix-helix domain. It is not known how an HTH DNA-binding domain affects higher-order structure for the HicAB modules. Here, we present crystal structures of the isolated E. coli HicB antitoxin and full-length HicAB complex showing that HicB forms a stable DNA-binding module and interacts in a canonical way with HicA despite the presence of an HTH-type DNA-binding domain. No major structural rearrangements take place upon binding of the toxin. Both structures expose well-ordered DNA-binding motifs allowing a model for DNA binding by the antitoxin to be generated.

Place, publisher, year, edition, pages
Elsevier, 2019. Vol. 27, no 11, p. 1675-+
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-166477DOI: 10.1016/j.str.2019.08.008ISI: 000494979900008PubMedID: 31495532OAI: oai:DiVA.org:umu-166477DiVA, id: diva2:1382179
Funder
Novo NordiskAvailable from: 2020-01-02 Created: 2020-01-02 Last updated: 2020-01-02Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Authority records BETA

Turnbull, Kathryn Jane

Search in DiVA

By author/editor
Turnbull, Kathryn JaneBrodersen, Ditlev Egeskov
In the same journal
Structure
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 2 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