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PMID: 2176161 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Identification by molecular cloning of two cDNA sequences from the plant Brassica napus which are very similar to mammalian protein phosphatases-1 and -2A.

FEBS letters ·Vol. 276 ·No. 1-2 ·1990-12-10 ·Pages 156-60

MacKintosh RW, Haycox G, Hardie DG, Cohen PT

Abstract

Two clones encoding protein phosphatase (PP) catalytic subunits have been isolated from a Brassica napus cDNA library screened with rabbit muscle PP1 alpha and PP2A alpha cDNAs. The deduced protein sequences are very similar to those of mammalian PP1 alpha and PP2A alpha (72% and 79% overall identity, respectively) indicating that they are the plant homologues of PP1 alpha and PP2A alpha. This high degree of similarity provides a molecular explanation for the remarkable conservation of the catalytic and regulatory properties between animal and plant protein phosphatases and supports the concept that PP1 and PP2A may be the most highly conserved of known enzymes.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Brassica/enzymology,genetics Chromosome Deletion Cloning, Molecular DNA/genetics,isolation & purification Gene Amplification Gene Library Molecular Sequence Data Phosphoprotein Phosphatases/genetics Rabbits Sequence Homology, Nucleic Acid
Chemicals
DNA Phosphoprotein Phosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
MacKintosh R W
Department of Biochemistry, University of Dundee, Scotland, UK.
Haycox G
Hardie D G
Cohen P T
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1990-12-10
Pages
156-60
Language
English
Region
England
NLM ID
0155157
Subset
IM
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