MoaB2, a newly identified transcription factor, binds to σ A in Mycobacterium smegmatis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00603767" target="_blank" >RIV/61388971:_____/24:00603767 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/24:00603767 RIV/61388963:_____/24:00603767 RIV/00216224:14740/24:00138935 RIV/00216208:11310/24:10497623

Výsledek na webu

<a href="https://journals.asm.org/doi/10.1128/jb.00066-24" target="_blank" >https://journals.asm.org/doi/10.1128/jb.00066-24</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/jb.00066-24" target="_blank" >10.1128/jb.00066-24</a>

Jazyk výsledku

angličtina

Název v původním jazyce

MoaB2, a newly identified transcription factor, binds to σ A in Mycobacterium smegmatis

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

MoaB2, a newly identified transcription factor, binds to σ A in Mycobacterium smegmatis

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Bacteriology

ISSN

0021-9193

e-ISSN

1098-5530

Svazek periodika

206

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

30

Strana od-do

e00066-24

Kód UT WoS článku

001348035500001

EID výsledku v databázi Scopus

2-s2.0-85213063372