All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

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

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Bacteriology

  • ISSN

    0021-9193

  • e-ISSN

    1098-5530

  • Volume of the periodical

    206

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    30

  • Pages from-to

    e00066-24

  • UT code for WoS article

    001348035500001

  • EID of the result in the Scopus database

    2-s2.0-85213063372