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.Základní údaje
Originální název
MoaB2, a newly identified transcription factor, binds to σA in Mycobacterium smegmatis
Autoři
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 ORCID; Martina JANOUSKOVA; Milada KAMBOVA; Petr HALADA; Alena KRENKOVA; Martin HUBALEK; Maria TRUNDOVA; Jan DOHNALEK; Jarmila HNILICOVA; Lukáš ŽÍDEK a Libor KRASNY
Vydání
Journal of Bacteriology, Washington, American Society for Microbiology, 2024, 0021-9193
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 3.000
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14740/24:00138935
Organizační jednotka
Středoevropský technologický institut
UT WoS
001348035500001
EID Scopus
2-s2.0-85213063372
Klíčová slova anglicky
MoaB2; sigma(A); mycobacteria; RNA polymerase; transcription
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 8. 12. 2025 10:21, Mgr. Eva Dubská
Anotace
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.
Návaznosti
| EF18_046/0015974, projekt VaV |
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| GA19-12956S, projekt VaV |
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| GA22-12023S, projekt VaV |
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| LM2018131, projekt VaV |
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| LX22NPO5103, projekt VaV |
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