Published online 18 February 2004
Nucleic Acids Research, 2004, Vol. 32, No. 3 1242-1250
© 2004 Oxford University Press
Mer1p is a modular splicing factor whose function depends on the conserved U2 snRNP protein Snu17p
1 Center for the Molecular Biology of RNA, Sinsheimer Laboratories, University of California, Santa Cruz, Santa Cruz, CA 95064, USA and 2 Department of Biology, University of Missouri, Saint Louis, 8001 Natural Bridge Road, Saint Louis, MO 63121, USA
*To whom correspondence should be addressed at Department of Biology, University of Missouri, Saint Louis, 8001 Natural Bridge Road, Saint Louis, MO 63121, USA. Tel: +1 314 516 6749; Fax: +1 314 516 6233; Email: spingola{at}umsl.edu
Mer1p activates the splicing of at least three pre-mRNAs (AMA1, MER2, MER3) during meiosis in the yeast Saccharomyces cerevisiae. We demonstrate that enhancer recognition by Mer1p is separable from Mer1p splicing activation. The C-terminal KH-type RNA-binding domain of Mer1p recognizes introns that contain the Mer1p splicing enhancer, while the N-terminal domain interacts with the spliceosome and activates splicing. Prior studies have implicated the U1 snRNP and recognition of the 5' splice site as key elements in Mer1p-activated splicing. We provide new evidence that Mer1p may also function at later steps of spliceosome assembly. First, Mer1p can activate splicing of introns that have mutated branch point sequences. Secondly, Mer1p fails to activate splicing in the absence of the non-essential U2 snRNP protein Snu17p. Thirdly, Mer1p interacts with the branch point binding proteins Mud2p and Bbp1p and the U2 snRNP protein Prp11p by two-hybrid assays. We conclude that Mer1p is a modular splicing regulator that can activate splicing at several early steps of spliceosome assembly and depends on the activities of both U1 and U2 snRNP proteins to activate splicing.
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