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.Základní údaje
Originální název
MoaB2, a newly identified transcription factor, binds to σA in Mycobacterium smegmatis
Autoři
BREZOVSKA, Barbora; Subhash NARASIMHAN (356 Indie, domácí); Michaela SIKOVA; Hana SANDEROVA; Tomas KOVAL; Nabajyoti BORAH; Mahmoud SHOMAN; Debora POSPISILOVA; Viola Vankova HAUSNEROVA; Dávid TUŽINČIN (703 Slovensko, domácí); Martin ČERNÝ (203 Česká republika, domácí); Jan KOMÁREK (203 Česká republika, domácí); Martina JANOUSKOVA; Milada KAMBOVA; Petr HALADA; Alena KRENKOVA; Martin HUBALEK; Maria TRUNDOVA; Jan DOHNALEK; Jarmila HNILICOVA; Lukáš ŽÍDEK (203 Česká republika, domácí) a Libor KRASNY
Vydání
Journal of Bacteriology, WASHINGTON, AMER SOC MICROBIOLOGY, 2024, 0021-9193
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Kód RIV
RIV/00216224:14740/24:00138935
Organizace
Středoevropský technologický institut – Masarykova univerzita – Repozitář
UT WoS
001348035500001
EID Scopus
2-s2.0-85213063372
Klíčová slova anglicky
MoaB2; sigma(A); mycobacteria; RNA polymerase; transcription
Návaznosti
EF18_046/0015974, projekt VaV. GA19-12956S, projekt VaV. GA22-12023S, projekt VaV. LM2018127, projekt VaV. LM2018131, projekt VaV. LX22NPO5103, projekt VaV. CIISB III, velká výzkumná infrastruktura.
Změněno: 4. 6. 2025 00:50, RNDr. Daniel Jakubík
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.