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Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.


ABSTRACT: WhiB7 represents a distinct subclass of transcription factors in the WhiB-Like (Wbl) family, a unique group of iron-sulfur (4Fe-4S] cluster-containing proteins exclusive to the phylum of Actinobacteria. In Mycobacterium tuberculosis (Mtb), WhiB7 interacts with domain 4 of the primary sigma factor (σA4) in the RNA polymerase holoenzyme and activates genes involved in multiple drug resistance and redox homeostasis. Here, we report crystal structures of the WhiB7:σA4 complex alone and bound to its target promoter DNA at 1.55-Å and 2.6-Å resolution, respectively. These structures show how WhiB7 regulates gene expression by interacting with both σA4 and the AT-rich sequence upstream of the -35 promoter DNA via its C-terminal DNA-binding motif, the AT-hook. By combining comparative structural analysis of the two high-resolution σA4-bound Wbl structures with molecular and biochemical approaches, we identify the structural basis of the functional divergence between the two distinct subclasses of Wbl proteins in Mtb.

SUBMITTER: Wan T 

PROVIDER: S-EPMC8876573 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

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Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.

Wan Tao T   Horová Magdaléna M   Beltran Daisy Guiza DG   Li Shanren S   Wong Huey-Xian HX   Zhang Li-Mei LM  

Molecular cell 20210624 14


WhiB7 represents a distinct subclass of transcription factors in the WhiB-Like (Wbl) family, a unique group of iron-sulfur (4Fe-4S] cluster-containing proteins exclusive to the phylum of Actinobacteria. In Mycobacterium tuberculosis (Mtb), WhiB7 interacts with domain 4 of the primary sigma factor (σ<sup>A</sup><sub>4</sub>) in the RNA polymerase holoenzyme and activates genes involved in multiple drug resistance and redox homeostasis. Here, we report crystal structures of the WhiB7:σ<sup>A</sup>  ...[more]

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