Přehled o publikaci
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.