The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain

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The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain. / Manav, Cemre; Turnbull, Kathryn Jane; Jurėnas, Dukas; Garcia-Pino, Abel; Gerdes, Kenn; Brodersen, Ditlev Egeskov.

In: Structure, Vol. 27, No. 11, 11.2019, p. 1675-1685.e3.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Manav, C, Turnbull, KJ, Jurėnas, D, Garcia-Pino, A, Gerdes, K & Brodersen, DE 2019, 'The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain', Structure, vol. 27, no. 11, pp. 1675-1685.e3. https://doi.org/10.1016/j.str.2019.08.008

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Author

Manav, Cemre ; Turnbull, Kathryn Jane ; Jurėnas, Dukas ; Garcia-Pino, Abel ; Gerdes, Kenn ; Brodersen, Ditlev Egeskov. / The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain. In: Structure. 2019 ; Vol. 27, No. 11. pp. 1675-1685.e3.

Bibtex

@article{ffc6a46f6fe94440bc6a61f6edeae2e3,
title = "The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain",
abstract = "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.",
keywords = "DNA-binding protein, RNase H, antitoxin, helix-turn-helix, ribbon-helix-helix, toxin",
author = "Cemre Manav and Turnbull, {Kathryn Jane} and Dukas Jurėnas and Abel Garcia-Pino and Kenn Gerdes and Brodersen, {Ditlev Egeskov}",
year = "2019",
month = "11",
doi = "10.1016/j.str.2019.08.008",
language = "English",
volume = "27",
pages = "1675--1685.e3",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "11",

}

RIS

TY - JOUR

T1 - The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain

AU - Manav, Cemre

AU - Turnbull, Kathryn Jane

AU - Jurėnas, Dukas

AU - Garcia-Pino, Abel

AU - Gerdes, Kenn

AU - Brodersen, Ditlev Egeskov

PY - 2019/11

Y1 - 2019/11

N2 - 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.

AB - 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.

KW - DNA-binding protein

KW - RNase H

KW - antitoxin

KW - helix-turn-helix

KW - ribbon-helix-helix

KW - toxin

UR - http://www.scopus.com/inward/record.url?scp=85074171976&partnerID=8YFLogxK

U2 - 10.1016/j.str.2019.08.008

DO - 10.1016/j.str.2019.08.008

M3 - Journal article

C2 - 31495532

VL - 27

SP - 1675-1685.e3

JO - Structure

JF - Structure

SN - 0969-2126

IS - 11

ER -