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

Skrisovska, L; Bourgeois, CF; Stefl, R; Grellscheid, SN; Kister, L; Wenter, P; Elliott, DJ; Stevenin, J; Allain, FH

Authors

L Skrisovska

CF Bourgeois

R Stefl

L Kister

P Wenter

DJ Elliott

J Stevenin

FH Allain



Abstract

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 CA/UCAA 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 β‐sheet surface binds to the RNA loop in a sequence‐specific fashion. Second, the β2–β3 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.

Journal Article Type Article
Publication Date 2007
Deposit Date Feb 11, 2013
Journal EMBO Reports
Print ISSN 1469-221X
Electronic ISSN 1469-3178
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 8
Issue 4
Pages 372-379
DOI https://doi.org/10.1038/sj.embor.7400910
Public URL https://durham-repository.worktribe.com/output/1468354