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; Michaela SIKOVA; Hana SANDEROVA; Tomas KOVAL; Nabajyoti BORAH; Mahmoud SHOMAN; Debora POSPISILOVA; Viola Vankova HAUSNEROVA; Dávid TUŽINČIN; Martin ČERNÝ; Jan KOMÁREK; Martina JANOUSKOVA; Milada KAMBOVA; Petr HALADA; Alena KRENKOVA; Martin HUBALEK; Maria TRUNDOVA; Jan DOHNALEK; Jarmila HNILICOVA; Lukáš ŽÍDEK 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:
Marked to be transferred to RIV
Yes
RIV identification code
RIV/00216224:14740/24:00138935
Organization
Středoevropský technologický institut – Repository – Repository
UT WoS
EID Scopus
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.
Changed: 9/12/2025 00:51, RNDr. Daniel Jakubík
Abstract
In the original language
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.
