Gle1 is required for tRNA to stimulate Dbp5 ATPase activity in vitro and promote Dbp5-mediated tRNA export in vivo in


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
08 Jan 2024
Historique:
medline: 9 1 2024
pubmed: 8 1 2024
entrez: 8 1 2024
Statut: epublish

Résumé

Cells must maintain a pool of processed and charged transfer RNAs (tRNA) to sustain translation capacity and efficiency. Numerous parallel pathways support the processing and directional movement of tRNA in and out of the nucleus to meet this cellular demand. Recently, several proteins known to control messenger RNA (mRNA) transport were implicated in tRNA export. The DEAD-box Protein 5, Dbp5, is one such example. In this study, genetic and molecular evidence demonstrates that Dbp5 functions parallel to the canonical tRNA export factor Los1. In vivo co-immunoprecipitation data further shows Dbp5 is recruited to tRNA independent of Los1, Msn5 (another tRNA export factor), or Mex67 (mRNA export adaptor), which contrasts with Dbp5 recruitment to mRNA that is abolished upon loss of Mex67 function. However, as with mRNA export, overexpression of Dbp5 dominant-negative mutants indicates a functional ATPase cycle and that binding of Dbp5 to Gle1 is required by Dbp5 to direct tRNA export. Biochemical characterization of the Dbp5 catalytic cycle demonstrates the direct interaction of Dbp5 with tRNA (or double-stranded RNA) does not activate Dbp5 ATPase activity, rather tRNA acts synergistically with Gle1 to fully activate Dbp5. These data suggest a model where Dbp5 directly binds tRNA to mediate export, which is spatially regulated via Dbp5 ATPase activation at nuclear pore complexes by Gle1.

Identifiants

pubmed: 38189406
doi: 10.7554/eLife.89835
pii: 89835
doi:
pii:

Substances chimiques

Adenosine Triphosphatases EC 3.6.1.-
Los1 protein, S cerevisiae 0
Nuclear Pore Complex Proteins 0
RNA, Messenger 0
RNA, Transfer 9014-25-9
Saccharomyces cerevisiae Proteins 0
GLE1 protein, S cerevisiae 0
DBP5 protein, S cerevisiae EC 3.6.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM145328
Pays : United States
Organisme : NIGMS NIH HHS
ID : GM007377
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35GM145328
Pays : United States

Informations de copyright

© 2023, Arul Nambi Rajan et al.

Déclaration de conflit d'intérêts

AA, RA, BM No competing interests declared

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Auteurs

Arvind Arul Nambi Rajan (A)

Biochemistry, Molecular, Cellular and Developmental Biology Graduate Group, University of California, Davis, Davis, United States.

Ryuta Asada (R)

Department of Viticulture and Enology, University of California, Davis, Davis, United States.

Ben Montpetit (B)

Biochemistry, Molecular, Cellular and Developmental Biology Graduate Group, University of California, Davis, Davis, United States.
Department of Viticulture and Enology, University of California, Davis, Davis, United States.

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Classifications MeSH