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Title

Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo
Authors
Kraemer, Angela
Legrain, P
Mulhauser, Frank
Groening, Karsten Johannes
Brosi, Reto
Bilbe, G
Published in Nucleic Acids Research. 1994, vol. 22, no. 24, p. 5223-8
Abstract A cDNA encoding the 60 kDa subunit of mammalian splicing factor SF3a has been isolated. The deduced protein sequence reveals a 30% identity to the PRP9 splicing protein of the yeast S.cerevisiae. The highest homology is present in a zinc finger-like region in the C-terminal domain of both proteins. The PRP9 zinc finger-like motif has been replaced by the equivalent region of mammalian SF3a60. The chimeric protein rescues the temperature-sensitive phenotype of the prp9-1 mutant strain demonstrating that not only the structure but also the function of this domain has been conserved during evolution.
Keywords Amino Acid Sequence — Base Sequence — Cloning, Molecular — DNA, Complementary/genetics — Escherichia coli/genetics — Fungal Proteins/genetics — Genes/genetics — Genes, Fungal/genetics — Hela Cells — Humans — Molecular Sequence Data — Molecular Weight — Mutation/physiology — Phenotype — RNA-Binding Proteins/chemistry/genetics/isolation & purification — Recombinant Fusion Proteins/biosynthesis — Ribonucleoprotein, U2 Small Nuclear — Saccharomyces cerevisiae/chemistry — Saccharomyces cerevisiae Proteins — Sequence Alignment — Sequence Analysis, DNA — Sequence Homology, Amino Acid — Zinc Fingers/genetics/physiology
Identifiers
PMID: 7816610
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Article (Published version) (1.3 MB) - private document Private access
Other version: http://preview.ncbi.nlm.nih.gov/pubmed/7816610
Structures
Faculté des sciences / Section de biologie / Département de biologie cellulaire
Citation
(ISO format) 		KRAEMER, Angela et al. Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo. In: Nucleic Acids Research, 1994, vol. 22, n° 24, p. 5223-8. https://archive-ouverte.unige.ch/unige:17580

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Deposited on : 2011-11-28

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