TY - JOUR
T1 - Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regionsin pre-mRNA
AU - Heinrich, Bettina
AU - Zhang, Zhaiyi
AU - Raitskin, Oleg
AU - Hiller, Michael
AU - Benderska, Natalya
AU - Hartmann, Annette M.
AU - Bracco, Laurent
AU - Elliott, David
AU - Ben-Ari, Shani
AU - Soreq, Hermona
AU - Sperling, Joseph
AU - Sperling, Ruth
AU - Stamm, Stefan
PY - 2009/5/22
Y1 - 2009/5/22
N2 - Almost every protein-coding gene undergoes pre-mRNA splicing, and the majority of these pre-mRNAs are alternatively spliced. Alternative exon usage is regulated by the transient formation of protein complexes on the pre-mRNA that typically contain heterogeneous nuclear ribonucleoproteins (hnRNPs). Here we characterize hnRNP G, a member of the hnRNP class of proteins. We show that hnRNP G is a nuclear protein that is expressed in different concentrations in various tissues and that interacts with other splicing regulatory proteins. hnRNP G is part of the supraspliceosome, where it regulates alternative splice site selection in a concentration-dependent manner. Its action on alternative exons can occur without a functional RNA-recognition motif by binding to other splicing regulatory proteins. The RNA-recognition motif of hnRNP G binds to a loose consensus sequence containing a CC(A/C) motif, and hnRNP G preferentially regulates alternative exons where this motif is clustered in close proximity. The X-chromosomally encoded hnRNP G regulates different RNAs than its Y-chromosomal paralogue RNA-binding motif protein, Y-linked (RBMY), suggesting that differences in alternative splicing, evoked by the sex-specific expression of hnRNP G and RBMY, could contribute to molecular sex differences in mammals.
AB - Almost every protein-coding gene undergoes pre-mRNA splicing, and the majority of these pre-mRNAs are alternatively spliced. Alternative exon usage is regulated by the transient formation of protein complexes on the pre-mRNA that typically contain heterogeneous nuclear ribonucleoproteins (hnRNPs). Here we characterize hnRNP G, a member of the hnRNP class of proteins. We show that hnRNP G is a nuclear protein that is expressed in different concentrations in various tissues and that interacts with other splicing regulatory proteins. hnRNP G is part of the supraspliceosome, where it regulates alternative splice site selection in a concentration-dependent manner. Its action on alternative exons can occur without a functional RNA-recognition motif by binding to other splicing regulatory proteins. The RNA-recognition motif of hnRNP G binds to a loose consensus sequence containing a CC(A/C) motif, and hnRNP G preferentially regulates alternative exons where this motif is clustered in close proximity. The X-chromosomally encoded hnRNP G regulates different RNAs than its Y-chromosomal paralogue RNA-binding motif protein, Y-linked (RBMY), suggesting that differences in alternative splicing, evoked by the sex-specific expression of hnRNP G and RBMY, could contribute to molecular sex differences in mammals.
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U2 - 10.1074/jbc.M901026200
DO - 10.1074/jbc.M901026200
M3 - Article
C2 - 19282290
AN - SCOPUS:67649831277
SN - 0021-9258
VL - 284
SP - 14303
EP - 14315
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 21
ER -