Transcriptome-scale analysis uncovers conserved residues in the hydrophobic core of the bacterial RNA chaperone Hfq required for small regulatory RNA stability

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F25%3A00619092" target="_blank" >RIV/68081707:_____/25:00619092 - isvavai.cz</a>

Výsledek na webu

<a href="https://academic.oup.com/nar/article/53/3/gkaf019/7983884?login=true" target="_blank" >https://academic.oup.com/nar/article/53/3/gkaf019/7983884?login=true</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/nar/gkaf019" target="_blank" >10.1093/nar/gkaf019</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Transcriptome-scale analysis uncovers conserved residues in the hydrophobic core of the bacterial RNA chaperone Hfq required for small regulatory RNA stability

Popis výsledku v původním jazyce

The Hfq protein, functioning as an RNA chaperone, plays a key role in the regulation of gene expression in bacteria and significantly facilitates the action of small regulatory RNAs (sRNAs). In our study, we created a systematic library of Hfq mutations, where individual amino acids were replaced by alanine, and these mutants were tested experimentally and using molecular dynamics methods. The results confirmed the key role of three RNA-binding surfaces for Hfq function. We discovered two previously undescribed, evolutionarily conserved amino acids – V22 and G34 – in the hydrophobic core of Hfq, which have a crucial impact on its ability to bind RNA inside the bacterial cell. Transcriptome analysis showed that the V22A and G34A mutations cause extensive destabilization of sRNA, to the same extent as in bacteria completely lacking Hfq. Nevertheless, these mutations led to only a slight change in the stability and structure of Hfq.

Název v anglickém jazyce

Transcriptome-scale analysis uncovers conserved residues in the hydrophobic core of the bacterial RNA chaperone Hfq required for small regulatory RNA stability

Popis výsledku anglicky

The Hfq protein, functioning as an RNA chaperone, plays a key role in the regulation of gene expression in bacteria and significantly facilitates the action of small regulatory RNAs (sRNAs). In our study, we created a systematic library of Hfq mutations, where individual amino acids were replaced by alanine, and these mutants were tested experimentally and using molecular dynamics methods. The results confirmed the key role of three RNA-binding surfaces for Hfq function. We discovered two previously undescribed, evolutionarily conserved amino acids – V22 and G34 – in the hydrophobic core of Hfq, which have a crucial impact on its ability to bind RNA inside the bacterial cell. Transcriptome analysis showed that the V22A and G34A mutations cause extensive destabilization of sRNA, to the same extent as in bacteria completely lacking Hfq. Nevertheless, these mutations led to only a slight change in the stability and structure of Hfq.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA23-05639S" target="_blank" >GA23-05639S: Molekulové simulace RNA: od statických struktur k molekulárním souborům</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

Nucleic Acids Research

ISSN

0305-1048

e-ISSN

1362-4962

Svazek periodika

53

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

16

Strana od-do

gkaf019

Kód UT WoS článku

001406930300001

EID výsledku v databázi Scopus

2-s2.0-85216631829