Detailed Information on Publication Record
2007
The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
SKRISOVSKA, Lenka, Cyril BOURGEOIS, Richard ŠTEFL, Sushma-Nagaraja GRELLSCHEID, Liliane KISTER et. al.Basic information
Original name
The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
Name in Czech
The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
Authors
SKRISOVSKA, Lenka (203 Czech Republic), Cyril BOURGEOIS (250 France), Richard ŠTEFL (203 Czech Republic, guarantor), Sushma-Nagaraja GRELLSCHEID (826 United Kingdom of Great Britain and Northern Ireland), Liliane KISTER (250 France), Philipp WENTER (756 Switzerland), David ELLIOTT (826 United Kingdom of Great Britain and Northern Ireland), James STEVENIN (250 France) and Frederic ALLAIN (250 France)
Edition
EMBO REPORTS, Nature Publishing Group, London, UK, Nature Publishing Group, London, UK, 2007, 1469-221X
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 7.450
RIV identification code
RIV/00216224:14310/07:00022207
Organization unit
Faculty of Science
UT WoS
000245359700017
Keywords in English
alternative splicing; NMR; protein-nucleic acid recognition; spermatogenesis; SELEX
Tags
International impact, Reviewed
Změněno: 29/6/2008 06:06, Olga Křížová
V originále
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.
In Czech
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.
Links
| MSM0021622413, plan (intention) |
|