Cef1p is a component of the Prp19p-associated complex and essential for pre-mRNA splicing

The Prp19p protein of the budding yeast Saccharomyces cerevisiae is an essential splicing factor and is associated with the spliceosome during the splicing reaction. We have previously shown that Prp19p is not tightly associated with small nuclear ribonucleoprotein particles but is associated with a...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 274; no. 14; pp. 9455 - 9462
Main Authors:	Tsai, W.Y. (National Yang-Ming University Shih-Pai, Taiwan, Republic of China.), Chow, Y.T, Chen, H.R, Huang, K.T, Hong, R.I, Jan, S.P, Kuo, N.Y, Tsao, T.Y, Chen, C.H, Cheng, S.C
Format:	Journal Article
Language:	English
Published:	United States American Society for Biochemistry and Molecular Biology 02-04-1999
Subjects:	ALTERNATIVE SPLICING Amino Acid Sequence ARN MENSAJERO ARN MESSAGER BINDING PROTEINS Cell Cycle Proteins - metabolism DNA BINDING MOTIFS Electrophoresis, Polyacrylamide Gel Fungal Proteins - metabolism Macromolecular Substances MESSENGER RNA Molecular Sequence Data PRECURSORS PROTEINAS AGLUTINANTES PROTEINE DE LIAISON RNA Precursors - metabolism RNA Splicing RNA Splicing Factors RNA-Binding Proteins SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae Proteins SPLICEOSOMES Spliceosomes - metabolism SPLICING FACTORS Structure-Activity Relationship Transcription Factors - metabolism
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Summary:	The Prp19p protein of the budding yeast Saccharomyces cerevisiae is an essential splicing factor and is associated with the spliceosome during the splicing reaction. We have previously shown that Prp19p is not tightly associated with small nuclear ribonucleoprotein particles but is associated with a protein complex consisting of at least eight protein components. By sequencing components of the affinity-purified complex, we have identified Cef1p as a component of the Prp19p-associated complex, Ntc85p. Cef1p could directly interact with Prp19p and was required for pre-mRNA splicing both in vivo and in vitro . The c-Myb DNA binding motif at the amino terminus of Cef1p was required for cellular growth but not for interaction of Cef1p with Prp19p or Cef1p self-interaction. We have identified a small region of 30 amino acid residues near the carboxyl terminus required for both cell viability and protein-protein interactions. Cef1p was associated with the spliceosome in the same manner as Prp19p, i.e. concomitant with or immediately after dissociation of U4. The anti-Cef1p antibody inhibited binding to the spliceosome of Cef1p, Prp19p, and at least three other components of the Prp19p-associated complex, suggesting that the Prp19p-associated complex is likely associated with the spliceosome and functions as an integral complex.
Bibliography:	1999010149 F30 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0021-9258 1083-351X
DOI:	10.1074/jbc.274.14.9455