The interaction between the F55 virus-encoded transcription regulator and the RadA host recombinase reveals a common strategy in Archaea and Bacteria to sense the UV-induced damage to the host DNA.


Journal

Biochimica et biophysica acta. Gene regulatory mechanisms
ISSN: 1876-4320
Titre abrégé: Biochim Biophys Acta Gene Regul Mech
Pays: Netherlands
ID NLM: 101731723

Informations de publication

Date de publication:
05 2020
Historique:
received: 21 11 2019
revised: 09 01 2020
accepted: 29 01 2020
pubmed: 6 2 2020
medline: 18 7 2020
entrez: 5 2 2020
Statut: ppublish

Résumé

Sulfolobus spindle-shaped virus 1 is the only UV-inducible member of the virus family Fuselloviridae. Originally isolated from Saccharolobus shibatae B12, it can also infect Saccharolobus solfataricus. Like the CI repressor of the bacteriophage λ, the SSV1-encoded F55 transcription repressor acts as a key regulator for the maintenance of the SSV1 carrier state. In particular, F55 binds to tandem repeat sequences located within the promoters of the early and UV-inducible transcripts. Upon exposure to UV light, a temporally coordinated pattern of gene expression is triggered. In the case of the better characterized bacteriophage λ, the switch from lysogenic to lytic development is regulated by a crosstalk between the virus encoded CI repressor and the host RecA, which regulates also the SOS response. For SSV1, instead, the regulatory mechanisms governing the switch from the carrier to the induced state have not been completely unravelled. In this study we have applied an integrated biochemical approach based on a variant of the EMSA assay coupled to mass spectrometry analyses to identify the proteins associated with F55 when bound to its specific DNA promoter sequences. Among the putative F55 interactors, we identified RadA and showed that the archaeal molecular components F55 and RadA are functional homologs of bacteriophage λ (factor CI) and Escherichia coli (RecA) system.

Identifiants

pubmed: 32014611
pii: S1874-9399(19)30442-0
doi: 10.1016/j.bbagrm.2020.194493
pii:
doi:

Substances chimiques

Archaeal Proteins 0
DNA-Binding Proteins 0
Escherichia coli Proteins 0
RadA protein, archaeal 0
Transcription Factors 0
Viral Proteins 0
recA protein, E coli 0
Rec A Recombinases EC 2.7.7.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

194493

Informations de copyright

Copyright © 2020. Published by Elsevier B.V.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Salvatore Fusco (S)

Department of Biology, University of Naples Federico II, 80126 Naples, Italy.

Martina Aulitto (M)

Department of Biology, University of Naples Federico II, 80126 Naples, Italy; Joint BioEnergy Institute, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

Ilaria Iacobucci (I)

Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy; CEINGE Advanced Biotechnologies, University of Naples Federico II, 80145 Naples, Italy.

Giulio Crocamo (G)

Department of Biology, University of Naples Federico II, 80126 Naples, Italy.

Pietro Pucci (P)

Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy; CEINGE Advanced Biotechnologies, University of Naples Federico II, 80145 Naples, Italy.

Simonetta Bartolucci (S)

Department of Biology, University of Naples Federico II, 80126 Naples, Italy.

Maria Monti (M)

Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy; CEINGE Advanced Biotechnologies, University of Naples Federico II, 80145 Naples, Italy. Electronic address: montimar@unina.it.

Patrizia Contursi (P)

Department of Biology, University of Naples Federico II, 80126 Naples, Italy. Electronic address: contursi@unina.it.

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Classifications MeSH