In vitro dimerization of human RIO2 kinase

Autor: Sébastien Fribourg, Stéphane Thore, Frédérique Maurice, Natacha Pérébaskine
Přispěvatelé: Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Acides Nucléiques : Régulations Naturelle et Artificielle (ARNA), Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), ARN : régulations naturelle et artificielle, Université Bordeaux Segalen - Bordeaux 2-Institut Européen de Chimie et de Biologie-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Université de Bordeaux (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Models
Molecular
Protein Conformation
Ribosome biogenesis
Protomer
In Vitro Techniques
Protein Serine-Threonine Kinases
Biology
Crystallography
X-Ray
Protein Structure
Secondary
Serine
03 medical and health sciences
Adenosine Triphosphate
0302 clinical medicine
Humans
Transferase
Threonine
Nuclear protein
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Protein kinase A
Molecular Biology
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
0303 health sciences
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
Kinase
Cell Biology
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
Biochemistry
030220 oncology & carcinogenesis
Protein Multimerization
Research Paper
Zdroj: RNA Biology
RNA Biology, Taylor & Francis, 2019, 16 (11), pp.1633-1642. ⟨10.1080/15476286.2019.1653679⟩
RNA Biol
ISSN: 1547-6286
1555-8584
DOI: 10.1080/15476286.2019.1653679⟩
Popis: RIO proteins form a conserved family of atypical protein kinases. RIO2 is a serine/threonine protein kinase/ATPase involved in pre-40S ribosomal maturation. Current crystal structures of archaeal and fungal Rio2 proteins report a monomeric form of the protein. Here, we describe three atomic structures of the human RIO2 kinase showing that it forms a homodimer in vitro. Upon self-association, each protomer ATP-binding pocket is partially remodelled and found in an apostate. The homodimerization is mediated by key residues previously shown to be responsible for ATP binding and catalysis. This unusual in vitro protein kinase dimer reveals an intricate mechanism where identical residues are involved in substrate binding and oligomeric state formation. We speculate that such an oligomeric state might be formed also in vivo and might function in maintaining the protein in an inactive state and could be employed during import.
Databáze: OpenAIRE
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