The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction

Autor: Sushma Nagaraja Grellscheid, Liliane Kister, Richard Štefl, Philipp Wenter, David J. Elliott, Lenka Skrisovska, James Stévenin, Cyril F. Bourgeois, Frédéric H.-T. Allain
Přispěvatelé: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des sciences et d'ing:nierie chimiques (ISIC), Ecole Polytechnique Fédérale de Lausanne (EPFL), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2007
Předmět:
Male
MESH: SELEX Aptamer Technique
MESH: Sequence Analysis
Protein
Scientific Report
Amino Acid Motifs
Molecular Sequence Data
MESH: Protein Structure
Secondary
RNA-binding protein
Electrophoretic Mobility Shift Assay
MESH: Amino Acid Sequence
Biology
Biochemistry
Protein Structure
Secondary
MESH: Amino Acid Motifs
Sequence Analysis
Protein
MESH: RNA
Testis
MESH: Directed Molecular Evolution
Genetics
Humans
Amino Acid Sequence
Nuclear protein
Molecular Biology
Gene
MESH: Mutagenesis
MESH: Humans
MESH: Molecular Sequence Data
RNA recognition motif
MESH: Testis
Alternative splicing
SELEX Aptamer Technique
RNA
Nuclear Proteins
RNA-Binding Proteins
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
Molecular biology
MESH: Male
Cell biology
MESH: RNA-Binding Proteins
Mutagenesis
RNA splicing
MESH: Electrophoretic Mobility Shift Assay
Directed Molecular Evolution
MESH: Nuclear Proteins
Systematic evolution of ligands by exponential enrichment
Zdroj: EMBO Reports
EMBO Reports, EMBO Press, 2007, 8 (4), pp.372-9. ⟨10.1038/sj.embor.7400910⟩
EMBO Reports, 2007, 8 (4), pp.372-9. ⟨10.1038/sj.embor.7400910⟩
ISSN: 1469-221X
1469-3178
DOI: 10.1038/sj.embor.7400910⟩
Popis: The RBMY (RNA-binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) participates in splicing in the testis. Using systematic evolution of ligands by exponential enrichment, we found that RNA stem-loops capped by a C(A)/(U)CAA pentaloop are high-affinity binding targets for hRBMY. Subsequent nuclear magnetic resonance structural determination of the hRBMY RNA recognition motif (RRM) in complex with a high-affinity target showed two distinct modes of RNA recognition. First, the RRM beta-sheet surface binds to the RNA loop in a sequence-specific fashion. Second, the beta2-beta3 loop of the hRBMY inserts into the major groove of the RNA stem. The first binding mode might be conserved in the paralogous protein heterogeneous nuclear RNP G, whereas the second mode of binding is found only in hRBMY. This structural difference could be at the origin of the function of RBMY in spermatogenesis.
Databáze: OpenAIRE
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