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Mutation in the prp12+ gene encoding a homolog of SAP130/SF3b130 causes differential inhibition of pre-mRNA splicing and arrest of cell-cycle progression in Schizosaccharomyces pombe

Published online by Cambridge University Press:  04 May 2001

YASUAKI HABARA ,
SEIICHI URUSHIYAMA ,
TOSHIHARU SHIBUYA ,
YASUMI OHSHIMA  and
TOKIO TANI
YASUAKI HABARA
Affiliation:
Department of Biology, Graduate School of Sciences, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan Present address: Howard Hughes Medical Institute (HHMI), Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
SEIICHI URUSHIYAMA
Affiliation:
Department of Biology, Graduate School of Sciences, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan Present address: Department of Molecular Cell Biology, Medical Research Institute, Tokyo Medical and Dental University, Kanda-Surugadai, Chiyoda 101-0062, Japan.
TOSHIHARU SHIBUYA
Affiliation:
Department of Biology, Graduate School of Sciences, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan
YASUMI OHSHIMA
Affiliation:
Department of Biology, Graduate School of Sciences, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan
TOKIO TANI
Affiliation:
Department of Biology, Graduate School of Sciences, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan PRESTO, Japan Science and Technology Corporation, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan
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Abstract

prp12-1 is one of the mutants defective in pre-mRNA splicing at a nonpermissive temperature in Schizosaccharomyces pombe. We found that the prp12+ gene encodes a protein highly homologous with a human splicing factor, SAP130/SF3b130, a subunit of a U2 snRNP-associated complex SF3b. Prp12p was shown to interact genetically with Prp10p that is a homolog of SAP155/SF3b155, another subunit in SF3b, suggesting that Prp12p is a functional homolog of human SAP130/SF3b130. Prp12p tagged with GFP is uniformly localized in the nuclear DNA region. In addition to pre-mRNA splicing defects, the prp12-1 mutant produced elongated cells, a typical phenotype of cell division cycle (cdc) mutants, suggesting a possible link between pre-mRNA splicing and cell-cycle progression. We examined kinetics of splicing defects in prp12-1 and several other prp mutants using northern blot hybridization and found that, among all the tested pre-mRNAs, only TfIId+ pre-mRNA with low splicing efficiency showed detectable splicing defects at the nonpermissive temperature in prp12-1. In addition, we found that other prp mutants with the cdc phenotype also showed differential splicing defects in tested pre-mRNAs at the nonpermissive temperature. On the other hand, prp mutants that do not exhibit the cdc phenotype showed a rapid and complete block of pre-mRNA splicing in all the tested pre-mRNAs at the nonpermissive temperature, indicating that prp mutants with weak splicing defects have a tendency to exhibit the cdc phenotype. These results suggest that the cdc phenotype in prp12-1 is caused by a selective reduction of spliced transcripts encoding a protein (or proteins) required for G2/M transition.

Keywords

cdcfission yeastintronmutantprpSF3bspliceosome associated protein
Type
Research Article
Information
RNA , Volume 7 , Issue 5 , May 2001 , pp. 671 - 681
Copyright
2001 RNA Society

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