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Article
Nature Structural & Molecular Biology 14, 597–603 (1 July 2007) | doi:10.1038/nsmb1263
RS domain|[ndash]|splicing signal interactions in splicing of U12-type and U2-type introns
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Abstract
Serine-arginine (SR) proteins are general metazoan splicing factors that contain an essential arginine/serine-rich (RS) domain. On typical U2-type introns, RS domains contact the branchpoint and 5|[prime]| splice site to promote base-pairing with U small nuclear RNAs (snRNAs). Here we analyze the role of SR proteins in splicing of U12-type introns and in the second step of U2-type intron splicing. We show that RS domains contact the branchpoint and 5|[prime]| splice site of a U12-type intron. On a U2-type intron, we find that the RS domain contacts the site of the U6 snRNA–5|[prime]| splice site interaction during the first step of splicing and shifts to contact the site of the U5 snRNA–exon 1 interaction during the second step. Our results reveal alternative interactions between the RS domain and 5|[prime]| splice site region that coincide with remodeling of the spliceosome between the two catalytic steps.
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