IronSulferCluV1, Main, Exploration, bibRecord, 000035

Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.

Identifieur interne : 000035 ( Main/Exploration ); précédent : 000034; suivant : 000036

Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.

Auteurs : Tao Wan ; Shanren Li ; Daisy Guiza Beltran ; Andrew Schacht ; Lu Zhang ; Donald F. Becker ; Limei Zhang [États-Unis]

Source :

Nucleic acids research [ 1362-4962 ] ; 2020.

RBID : pubmed:31807774

Descripteurs français

English descriptors

KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Crystallography, X-Ray (MeSH), Gene Expression Regulation, Bacterial (genetics), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Mycobacterium tuberculosis (chemistry), Mycobacterium tuberculosis (genetics), Mycobacterium tuberculosis (pathogenicity), Promoter Regions, Genetic (MeSH), Protein Conformation (MeSH), Sigma Factor (chemistry), Sigma Factor (genetics), Transcription Factors (chemistry), Transcription Factors (genetics), Transcription, Genetic (MeSH), Tuberculosis (genetics), Tuberculosis (microbiology).
MESH :
- chemical , chemistry : Bacterial Proteins, Iron-Sulfur Proteins, Sigma Factor, Transcription Factors.
- chemical , genetics : Bacterial Proteins, Iron-Sulfur Proteins, Sigma Factor, Transcription Factors.
- chemistry : Mycobacterium tuberculosis.
- genetics : Gene Expression Regulation, Bacterial, Mycobacterium tuberculosis, Tuberculosis.
- microbiology : Tuberculosis.
- pathogenicity : Mycobacterium tuberculosis.
- Crystallography, X-Ray, Humans, Promoter Regions, Genetic, Protein Conformation, Transcription, Genetic.

Abstract

WhiB1 is a monomeric iron-sulfur cluster-containing transcription factor in the WhiB-like family that is widely distributed in actinobacteria including the notoriously persistent pathogen Mycobacterium tuberculosis (M. tuberculosis). WhiB1 plays multiple roles in regulating cell growth and responding to nitric oxide stress in M. tuberculosis, but its underlying mechanism is unclear. Here we report a 1.85 Å-resolution crystal structure of the [4Fe-4S] cluster-bound (holo-) WhiB1 in complex with the C-terminal domain of the σ70-family primary sigma factor σA of M. tuberculosis containing the conserved region 4 (σA4). Region 4 of the σ70-family primary sigma factors is commonly used by transcription factors for gene activation, and holo-WhiB1 has been proposed to activate gene expression via binding to σA4. The complex structure, however, unexpectedly reveals that the interaction between WhiB1 and σA4 is dominated by hydrophobic residues in the [4Fe-4S] cluster binding pocket, distinct from previously characterized canonical σ704-bound transcription activators. Furthermore, we show that holo-WhiB1 represses transcription by interaction with σA4in vitro and that WhiB1 must interact with σA4 to perform its essential role in supporting cell growth in vivo. Together, these results demonstrate that holo-WhiB1 regulates gene expression by a non-canonical mechanism relative to well-characterized σA4-dependent transcription activators.

DOI: 10.1093/nar/gkz1133
PubMed: 31807774
PubMed Central: PMC6954389

Affiliations:

Links toward previous steps (curation, corpus...)

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to stream Main, to step Curation: 000180

Le document en format XML

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<term>Bacterial Proteins (genetics)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Gene Expression Regulation, Bacterial (genetics)</term>
<term>Humans (MeSH)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Mycobacterium tuberculosis (chemistry)</term>
<term>Mycobacterium tuberculosis (genetics)</term>
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<term>Sigma Factor (genetics)</term>
<term>Transcription Factors (chemistry)</term>
<term>Transcription Factors (genetics)</term>
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<term>Tuberculosis (genetics)</term>
<term>Tuberculosis (microbiology)</term>
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<term>Facteur sigma (composition chimique)</term>
<term>Facteur sigma (génétique)</term>
<term>Facteurs de transcription (composition chimique)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Humains (MeSH)</term>
<term>Mycobacterium tuberculosis (composition chimique)</term>
<term>Mycobacterium tuberculosis (génétique)</term>
<term>Mycobacterium tuberculosis (pathogénicité)</term>
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<term>Protéines bactériennes (génétique)</term>
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<term>Régulation de l'expression des gènes bactériens (génétique)</term>
<term>Transcription génétique (MeSH)</term>
<term>Tuberculose (génétique)</term>
<term>Tuberculose (microbiologie)</term>
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<term>Ferrosulfoprotéines</term>
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<term>Protéines bactériennes</term>
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<front><div type="abstract" xml:lang="en">WhiB1 is a monomeric iron-sulfur cluster-containing transcription factor in the WhiB-like family that is widely distributed in actinobacteria including the notoriously persistent pathogen Mycobacterium tuberculosis (M. tuberculosis). WhiB1 plays multiple roles in regulating cell growth and responding to nitric oxide stress in M. tuberculosis, but its underlying mechanism is unclear. Here we report a 1.85 Å-resolution crystal structure of the [4Fe-4S] cluster-bound (holo-) WhiB1 in complex with the C-terminal domain of the σ70-family primary sigma factor σA of M. tuberculosis containing the conserved region 4 (σA4). Region 4 of the σ70-family primary sigma factors is commonly used by transcription factors for gene activation, and holo-WhiB1 has been proposed to activate gene expression via binding to σA4. The complex structure, however, unexpectedly reveals that the interaction between WhiB1 and σA4 is dominated by hydrophobic residues in the [4Fe-4S] cluster binding pocket, distinct from previously characterized canonical σ704-bound transcription activators. Furthermore, we show that holo-WhiB1 represses transcription by interaction with σA4in vitro and that WhiB1 must interact with σA4 to perform its essential role in supporting cell growth in vivo. Together, these results demonstrate that holo-WhiB1 regulates gene expression by a non-canonical mechanism relative to well-characterized σA4-dependent transcription activators.</div>
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<Abstract><AbstractText>WhiB1 is a monomeric iron-sulfur cluster-containing transcription factor in the WhiB-like family that is widely distributed in actinobacteria including the notoriously persistent pathogen Mycobacterium tuberculosis (M. tuberculosis). WhiB1 plays multiple roles in regulating cell growth and responding to nitric oxide stress in M. tuberculosis, but its underlying mechanism is unclear. Here we report a 1.85 Å-resolution crystal structure of the [4Fe-4S] cluster-bound (holo-) WhiB1 in complex with the C-terminal domain of the σ70-family primary sigma factor σA of M. tuberculosis containing the conserved region 4 (σA4). Region 4 of the σ70-family primary sigma factors is commonly used by transcription factors for gene activation, and holo-WhiB1 has been proposed to activate gene expression via binding to σA4. The complex structure, however, unexpectedly reveals that the interaction between WhiB1 and σA4 is dominated by hydrophobic residues in the [4Fe-4S] cluster binding pocket, distinct from previously characterized canonical σ704-bound transcription activators. Furthermore, we show that holo-WhiB1 represses transcription by interaction with σA4in vitro and that WhiB1 must interact with σA4 to perform its essential role in supporting cell growth in vivo. Together, these results demonstrate that holo-WhiB1 regulates gene expression by a non-canonical mechanism relative to well-characterized σA4-dependent transcription activators.</AbstractText>
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   |texte=   Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.
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Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.

Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.

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