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Characterization of a transitionally occupied state and thermal unfolding of domain 1.1 of s(A) factor of RNA polymerase from Bacillus subtilis

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F23%3A00575354" target="_blank" >RIV/61388971:_____/23:00575354 - isvavai.cz</a>

  • Výsledek na webu

    <a href="https://onlinelibrary.wiley.com/doi/10.1002/prot.26531" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/prot.26531</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/prot.26531" target="_blank" >10.1002/prot.26531</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Characterization of a transitionally occupied state and thermal unfolding of domain 1.1 of s(A) factor of RNA polymerase from Bacillus subtilis

  • Popis výsledku v původním jazyce

    sigma factors are essential parts of bacterial RNA polymerase (RNAP) as they allow to recognize promotor sequences and initiate transcription. Domain 1.1 of vegetative sigma factors occupies the primary channel of RNAP and also prevents binding of the sigma factor to promoter DNA alone. Here, we show that domain 1.1 of Bacillus subtilis sigma(A) exists in more structurally distinct variants in dynamic equilibrium. The major conformation at room temperature is represented by a previously reported well-folded structure solved by nuclear magnetic resonance (NMR), but 4% of the protein molecules are present in a less thermodynamically favorable state. We show that this population increases with temperature and we predict its significant elevation at higher but still biologically relevant temperatures. We characterized the minor state of the domain 1.1 using specialized methods of NMR. We found that, in contrast to the major state, the detected minor state is partially unfolded. Its propensity to form secondary structure elements is especially decreased for the first and third alpha helices, while the second alpha helix and ss strand close to the C-terminus are more stable. We also analyzed thermal unfolding of the domain 1.1 and performed functional experiments with full length sigma(A) and its shortened version lacking domain 1.1 ((sigma A_Delta 1:1)). The results revealed that while full length sA increases transcription activity of RNAP with increasing temperature, transcription with (sigma A_Delta 1:1) remains constant. In summary, this study reveals conformational dynamics of domain 1.1 and provides a basis for studies of its interaction with RNAP and effects on transcription regulation.

  • Název v anglickém jazyce

    Characterization of a transitionally occupied state and thermal unfolding of domain 1.1 of s(A) factor of RNA polymerase from Bacillus subtilis

  • Popis výsledku anglicky

    sigma factors are essential parts of bacterial RNA polymerase (RNAP) as they allow to recognize promotor sequences and initiate transcription. Domain 1.1 of vegetative sigma factors occupies the primary channel of RNAP and also prevents binding of the sigma factor to promoter DNA alone. Here, we show that domain 1.1 of Bacillus subtilis sigma(A) exists in more structurally distinct variants in dynamic equilibrium. The major conformation at room temperature is represented by a previously reported well-folded structure solved by nuclear magnetic resonance (NMR), but 4% of the protein molecules are present in a less thermodynamically favorable state. We show that this population increases with temperature and we predict its significant elevation at higher but still biologically relevant temperatures. We characterized the minor state of the domain 1.1 using specialized methods of NMR. We found that, in contrast to the major state, the detected minor state is partially unfolded. Its propensity to form secondary structure elements is especially decreased for the first and third alpha helices, while the second alpha helix and ss strand close to the C-terminus are more stable. We also analyzed thermal unfolding of the domain 1.1 and performed functional experiments with full length sigma(A) and its shortened version lacking domain 1.1 ((sigma A_Delta 1:1)). The results revealed that while full length sA increases transcription activity of RNAP with increasing temperature, transcription with (sigma A_Delta 1:1) remains constant. In summary, this study reveals conformational dynamics of domain 1.1 and provides a basis for studies of its interaction with RNAP and effects on transcription regulation.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10606 - Microbiology

Návaznosti výsledku

  • Projekt

    <a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

  • Návaznosti

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Ostatní

  • Rok uplatnění

    2023

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    Proteins-Structure, Function and Bioinformatics

  • ISSN

    0887-3585

  • e-ISSN

    1097-0134

  • Svazek periodika

    91

  • Číslo periodika v rámci svazku

    9

  • Stát vydavatele periodika

    US - Spojené státy americké

  • Počet stran výsledku

    12

  • Strana od-do

    1276-1287

  • Kód UT WoS článku

    001019240900001

  • EID výsledku v databázi Scopus

    2-s2.0-85162675407