Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue

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 compri...

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Bibliographic Details
Published in:Nucleic acids research 1997-03, Vol.25 (5), p.1028-1035
Main Authors: Gross, T, Lutzelberger, M, Wiegmann, H, Klingenhoff, A, Shenoy, S, Kaufer, N.F
Format: Article
Language:English
Subjects:
alternative splicing
Amino Acid Sequence
amino acid sequences
Animals
binding proteins
Binding Sites
complementary DNA
DNA Primers
DNA, Complementary
enzyme activity
genbank/l10739
genbank/u488736 [sic]
genbank/u488737 [sic]
genbank/u66833
genetic complementation
Genetic Complementation Test
HeLa Cells
Humans
Mammals
messenger RNA
Mice
Mitosis
Molecular Sequence Data
Mutagenesis, Site-Directed
mutation
Nuclear Proteins - metabolism
nucleotide sequences
phosphorylation
precursors
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
prp4 gene
Rabbits
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
recombinant proteins
Ribonucleoprotein, U4-U6 Small Nuclear - genetics
Ribonucleoprotein, U4-U6 Small Nuclear - metabolism
RNA Precursors - metabolism
RNA Splicing
RNA Splicing Factors
RNA-Binding Proteins
Schizosaccharomyces - enzymology
Schizosaccharomyces - genetics
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins
Sequence Homology, Amino Acid
Serine-Arginine Splicing Factors
species differences
splicing factors
structural genes
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Summary: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
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/25.5.1028