The RNA repair proteins RtcAB regulate transcription activator RtcR via its CRISPR-associated Rossmann fold domain.

Cell biology Molecular biology Molecular mechanism of gene regulation

Journal

iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038

Informations de publication

Date de publication:
18 Nov 2022
Historique:
received: 24 01 2022
revised: 21 05 2022
accepted: 18 10 2022
entrez: 17 11 2022
pubmed: 18 11 2022
medline: 18 11 2022
Statut: epublish

Résumé

CRISPR-associated Rossmann fold (CARF) domain signaling underpins modulation of CRISPR-Cas nucleases; however, the RtcR CARF domain controls expression of two conserved RNA repair enzymes, cyclase RtcA and ligase RtcB. Here, we demonstrate that RtcAB are required for RtcR-dependent transcription activation and directly bind to RtcR CARF. RtcAB catalytic activity is not required for complex formation with CARF, but is essential yet not sufficient for RtcRAB-dependent transcription activation, implying the need for an additional RNA repair-dependent activating signal. This signal differs from oligoadenylates, a known ligand of CARF domains, and instead appears to originate from the translation apparatus: RtcB repairs a tmRNA that rescues stalled ribosomes and increases translation elongation speed. Taken together, our data provide evidence for an expanded range for CARF domain signaling, including the first evidence of its control via

Identifiants

pubmed: 36388977
doi: 10.1016/j.isci.2022.105425
pii: S2589-0042(22)01697-2
pmc: PMC9650030
doi:

Types de publication

Journal Article

Langues

eng

Pagination

105425

Informations de copyright

© 2022 The Authors.

Déclaration de conflit d'intérêts

The authors declare no competing interests.

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Auteurs

Ioly Kotta-Loizou (I)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.

Maria Grazia Giuliano (MG)

School of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, UK.

Milija Jovanovic (M)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.

Jorrit Schaefer (J)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.

Fuzhou Ye (F)

Section of Structural Biology, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK.

Nan Zhang (N)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
Houston Methodist Research Institute, Houston, TX 77030, USA.

Danai Athina Irakleidi (DA)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.

Xiaojiao Liu (X)

Section of Structural Biology, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK.
College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China.

Xiaodong Zhang (X)

Section of Structural Biology, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK.

Martin Buck (M)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.

Christoph Engl (C)

Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
School of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, UK.

Classifications MeSH