The small DUF1127 protein CcaF1 from Rhodobacter sphaeroides is an RNA-binding protein involved in sRNA maturation and RNA turnover.
Alphaproteobacteria
/ genetics
Bacterial Proteins
/ metabolism
Computer Simulation
Endoribonucleases
/ physiology
Gene Expression Regulation, Bacterial
RNA Processing, Post-Transcriptional
RNA Stability
RNA, Bacterial
/ metabolism
RNA, Small Untranslated
/ metabolism
RNA-Binding Proteins
/ metabolism
Rhodobacter sphaeroides
/ genetics
Stress, Physiological
Transcriptome
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
06 04 2021
06 04 2021
Historique:
accepted:
26
02
2021
revised:
10
02
2021
received:
17
06
2020
pubmed:
12
3
2021
medline:
13
5
2021
entrez:
11
3
2021
Statut:
ppublish
Résumé
Many different protein domains are conserved among numerous species, but their function remains obscure. Proteins with DUF1127 domains number >17 000 in current databases, but a biological function has not yet been assigned to any of them. They are mostly found in alpha- and gammaproteobacteria, some of them plant and animal pathogens, symbionts or species used in industrial applications. Bioinformatic analyses revealed similarity of the DUF1127 domain of bacterial proteins to the RNA binding domain of eukaryotic Smaug proteins that are involved in RNA turnover and have a role in development from Drosophila to mammals. This study demonstrates that the 71 amino acid DUF1127 protein CcaF1 from the alphaproteobacterium Rhodobacter sphaeroides participates in maturation of the CcsR sRNAs that are processed from the 3' UTR of the ccaF mRNA and have a role in the oxidative stress defense. CcaF1 binds to many cellular RNAs of different type, several mRNAs with a function in cysteine / methionine / sulfur metabolism. It affects the stability of the CcsR RNAs and other non-coding RNAs and mRNAs. Thus, the widely distributed DUF1127 domain can mediate RNA-binding, affect stability of its binding partners and consequently modulate the bacterial transcriptome, thereby influencing different physiological processes.
Identifiants
pubmed: 33706375
pii: 6168310
doi: 10.1093/nar/gkab146
pmc: PMC8034643
doi:
Substances chimiques
Bacterial Proteins
0
RNA, Bacterial
0
RNA, Small Untranslated
0
RNA-Binding Proteins
0
Endoribonucleases
EC 3.1.-
ribonuclease E
EC 3.1.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3003-3019Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.
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