Fission yeast Prp4p kinase regulates pre-mRNA splicing by phosphorylating a non-SR-splicing factor.

Autor:	Schwelnus, Wiebke, Richert, Kathrin, Opitz, Florian, Groβ, Thomas, Habara, Yasuaki, Tani, Tokio, Käufer, Norbert F.
Předmět:	RNA PHOSPHORYLATION YEAST CELL cycle BACTERIA PROTEINS
Zdroj:	EMBO Reports; Jan2001, Vol. 2 Issue 1, p35-41, 7p
Abstrakt:	We provide evidence that Prp4p kinase activity is required for pre-mRNA splicing in vivo and show that loss of activity impairs G1-S and G2-M progression in the cell cycle. Prp4p interacts genetically with the non-SR (serine/arginine) splicing factors Prplp and Prpsp. Bacterially produced Prplp is phosphorylated by Prp4p in vitro. Prp4p and Prpl p also interact in the yeast two-hybrid system. In vivo labelling studies using a strain with a mutant allele of the prp4 gene in the genetic background indicate a change in phosphorylation of the Prplp protein. These results are consistent with the notion that Prp4p kinase is involved in the control of the formation of active spliceosomes, targeting non-SR splicing factors. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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