J 2024

MoaB2, a newly identified transcription factor, binds to σA in Mycobacterium smegmatis

BREZOVSKA, Barbora; Subhash NARASIMHAN; Michaela SIKOVA; Hana SANDEROVA; Tomas KOVAL et. al.

Basic information

Original name

MoaB2, a newly identified transcription factor, binds to σA in Mycobacterium smegmatis

Authors

BREZOVSKA, Barbora; Subhash NARASIMHAN (356 India, belonging to the institution); Michaela SIKOVA; Hana SANDEROVA; Tomas KOVAL; Nabajyoti BORAH; Mahmoud SHOMAN; Debora POSPISILOVA; Viola Vankova HAUSNEROVA; Dávid TUŽINČIN (703 Slovakia, belonging to the institution); Martin ČERNÝ (203 Czech Republic, belonging to the institution); Jan KOMÁREK (203 Czech Republic, belonging to the institution); Martina JANOUSKOVA; Milada KAMBOVA; Petr HALADA; Alena KRENKOVA; Martin HUBALEK; Maria TRUNDOVA; Jan DOHNALEK; Jarmila HNILICOVA; Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution) and Libor KRASNY

Edition

Journal of Bacteriology, WASHINGTON, AMER SOC MICROBIOLOGY, 2024, 0021-9193

Other information

Language

English

Type of outcome

Article in a journal

Country of publisher

United States of America

Confidentiality degree

is not subject to a state or trade secret

References:

RIV identification code

RIV/00216224:14740/24:00138935

Organization

Středoevropský technologický institut – Repository – Repository

UT WoS

001348035500001

EID Scopus

2-s2.0-85213063372

Keywords in English

MoaB2; sigma(A); mycobacteria; RNA polymerase; transcription

Links

EF18_046/0015974, research and development project. GA19-12956S, research and development project. GA22-12023S, research and development project. LM2018127, research and development project. LM2018131, research and development project. LX22NPO5103, research and development project. CIISB III, large research infrastructures.
Changed: 4/6/2025 00:50, RNDr. Daniel Jakubík

Abstract

V originále

In mycobacteria, σA is the primary sigma factor. This essential protein binds to RNA polymerase (RNAP) and mediates transcription initiation of housekeeping genes. Our knowledge about this factor in mycobacteria is limited. Here, we performed an unbiased search for interacting partners of Mycobacterium smegmatis σA. The search revealed a number of proteins; prominent among them was MoaB2. The σA-MoaB2 interaction was validated and characterized by several approaches, revealing that it likely does not require RNAP and is specific, as alternative σ factors (e.g., closely related σB) do not interact with MoaB2. The structure of MoaB2 was solved by X-ray crystallography. By immunoprecipitation and nuclear magnetic resonance, the unique, unstructured N-terminal domain of σA was identified to play a role in the σA-MoaB2 interaction. Functional experiments then showed that MoaB2 inhibits σA-dependent (but not σB-dependent) transcription and may increase the stability of σA in the cell. We propose that MoaB2, by sequestering σA, has a potential to modulate gene expression. In summary, this study has uncovered a new binding partner of mycobacterial σA, paving the way for future investigation of this phenomenon.

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