Complementation of the cs dis2-11 cell cycle mutant of Schizosaccharomyces pombe by a protein phosphatase from Arabidopsis thaliana.

doi:10.1002/j.1460-2075.1992.tb05177.x

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Article

Complementation of the cs dis2-11 cell cycle mutant of Schizosaccharomyces pombe by a protein phosphatase from Arabidopsis thaliana.

The EMBO journal - 1 Apr 1992

Nitschke K, Fleig U, Schell J, Palme K

Abstract excerpt

The activities of type I protein phosphatases play a central role in eukaryotic cell cycle control. Here, we report the cloning and characterization from the flowering plant Arabidopsis thaliana of a cDNA clone named PP1-At which is highly homologous to protein phosphatase 1. The deduced amino acid sequence of PP1-At shows that the PP1-At protein is 318 amino acid residues long and has a molecular weight of...

Topics

Amino Acid Sequence
Animals
Base Sequence
Cell Cycle
Cloning, Molecular
Cold Temperature
DNA
Genes, Dominant
Genes, Plant
Genetic Complementation Test
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Oligodeoxyribonucleotides

Phosphoprotein Phosphatases

Plants

Polymerase Chain Reaction

Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 1314161
DOI: 10.1002/j.1460-2075.1992.tb05177.x
PMCID: PMC556581

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1314161-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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