Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
24 01 2020
24 01 2020
Historique:
accepted:
18
11
2019
revised:
12
11
2019
received:
24
06
2019
pubmed:
5
12
2019
medline:
19
3
2020
entrez:
5
12
2019
Statut:
ppublish
Résumé
In all organisms, a selected type of proteins accomplishes critical roles in cellular processes that govern gene expression. The multifunctional protein Gemin5 cooperates in translation control and ribosome binding, besides acting as the RNA-binding protein of the survival of motor neuron (SMN) complex. While these functions reside on distinct domains located at each end of the protein, the structure and function of the middle region remained unknown. Here, we solved the crystal structure of an extended tetratricopeptide (TPR)-like domain in human Gemin5 that self-assembles into a previously unknown canoe-shaped dimer. We further show that the dimerization module is functional in living cells driving the interaction between the viral-induced cleavage fragment p85 and the full-length Gemin5, which anchors splicing and translation members. Disruption of the dimerization surface by a point mutation in the TPR-like domain prevents this interaction and also abrogates translation enhancement induced by p85. The characterization of this unanticipated dimerization domain provides the structural basis for a role of the middle region of Gemin5 as a central hub for protein-protein interactions.
Identifiants
pubmed: 31799608
pii: 5651328
doi: 10.1093/nar/gkz1126
pmc: PMC6954437
doi:
Substances chimiques
GEMIN5 protein, human
0
RNA-Binding Proteins
0
Ribonucleoproteins, Small Nuclear
0
SMN Complex Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
788-801Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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