0603767 - MBÚ 2025 RIV US eng J - Journal Article
Brezovská, Barbora - Narasimhan, S. - Šiková, Michaela - Šanderová, Hana - Kovaľ, Tomáš - Borah, Nabajyoti - Shoman, Mahmoud - Pospíšilová, Debora - Hausnerová Vaňková, Viola - Tužinčin, D. - Černý, M. - Komárek, J. - Janoušková, Martina - Kambová, Milada - Halada, Petr - Křenková, Alena - Hubálek, Martin - Trundová, Mária - Dohnálek, Jan - Hnilicová, Jarmila - Zídek, L. - Krásný, Libor
MoaB2, a newly identified transcription factor, binds to σ A in Mycobacterium smegmatis.
Journal of Bacteriology. Roč. 206, č. 12 (2024). ISSN 0021-9193. E-ISSN 1098-5530
R&D Projects: GA ČR(CZ) GA19-12956S; GA ČR(CZ) GA22-12023S; GA ČR(CZ) GA23-05622S; GA MŠMT(CZ) LX22NPO5103; GA MŠMT(CZ) LM2018131; GA MŠMT LM2023042; GA MŠMT(CZ) LM2018127; GA MŠMT(CZ) EF18_046/0015974
Research Infrastructure: CIISB III - 90242; CIISB II - 90127
Institutional support: RVO:61388971 ; RVO:86652036 ; RVO:61388963
Keywords : escherichia-coli regulator * rna-polymerase * bacillus-subtilis * crystal-structure * stress-response * differential expression * stationary-phase * larger proteins * tuberculosis * molybdenum * MoaB2 * sigma(A) * mycobacteria * RNA polymerase * transcription
OECD category: Microbiology; Microbiology (UOCHB-X)
Impact factor: 2.7, year: 2023 ; AIS: 0.917, rok: 2023
Method of publishing: Open access
Result website:
https://journals.asm.org/doi/10.1128/jb.00066-24DOI: https://doi.org/10.1128/jb.00066-24

In mycobacteria, sigma(A) 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 sigma(A). The search revealed a number of proteins, prominent among them was MoaB2. The sigma(A)-MoaB2 interaction was validated and characterized by several approaches, revealing that it likely does not require RNAP and is specific, as alternative sigma factors (e.g., closely related sigma(B)) 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 sigma(A) was identified to play a role in the sigma(A)-MoaB2 interaction. Functional experiments then showed that MoaB2 inhibits sigma(A)-dependent (but not sigma(B)-dependent) transcription and may increase the stability of sigma(A) in the cell. We propose that MoaB2, by sequestering sigma(A), has a potential to modulate gene expression. In summary, this study has uncovered a new binding partner of mycobacterial sigma(A), paving the way for future investigation of this phenomenon.br / IMPORTANCE Mycobacteria cause serious human diseases such as tuberculosis and leprosy. The mycobacterial transcription machinery is unique, containing transcription factors such as RbpA, CarD, and the RNA polymerase (RNAP) core-interacting small RNA Ms1. Here, we extend our knowledge of the mycobacterial transcription apparatus by identifying MoaB2 as an interacting partner of sigma(A), the primary sigma factor, and characterize its effects on transcription and sigma(A) stability. This information expands our knowledge of interacting partners of subunits of mycobacterial RNAP, providing opportunities for future development of antimycobacterial compounds.
Permanent Link: https://hdl.handle.net/11104/0361080