Nucleic Acids Research, Vol 25, Issue 5 1028-1035, Copyright © 1997 by Oxford University Press
T Gross, M Lutzelberger, H Weigmann, A Klingenhoff, S Shenoy and NF Kaufer
The prp4 gene of Schizosaccharomyces pombe encodes a protein kinase. A
physiological substrate is not yet known. A mutational analysis of prp4
revealed that the protein consists of a short N-terminal domain, containing
several essential motifs, which is followed by the kinase catalytic domain
comprising the C-terminus of the protein. Overexpression of N-terminal
mutations disturbs mitosis and produces elongated cells, Using a PCR
approach, we isolated a putative homologue of Prp4 from human and mouse
cells. The mammalian kinase domain is 53% identical to the kinase domain of
Prp4. The short N-terminal domains share <20% identical amino acids, but
contain conserved motifs. A fusion protein consisting of the N-terminal
region from S. pombe followed by the mammalian kinase domain complements a
temperature- sensitive prp4 mutation of S. pombe. Prp4 and the recombinant
yeast/mouse protein kinase phosphorylate the human SR splicing factor
ASF/SF2 in vitro in its RS domain.
ARTICLES
Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue
Institut fur Genetik-Biozentrum, Technische Universitat Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany.
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