Title : Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A.

Pub. Date : 1996 Jun

PMID : 8799831






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 We show here that okadaic acid and microcystin-LR block the in vitro dephosphorylation of H1 and that they do so directly by inhibiting the histone H1 phosphatase rather than by some indirect mechanism. Okadaic Acid H1.0 linker histone Homo sapiens
2 The concentrations of microcystin and okadaic acid required for inhibition strongly suggest that the histone H1 phosphatase is either PP1 or an unknown protein phosphatase with okadaic acid-sensitivity similar to PP1. Okadaic Acid H1.0 linker histone Homo sapiens
3 The concentrations of microcystin and okadaic acid required for inhibition strongly suggest that the histone H1 phosphatase is either PP1 or an unknown protein phosphatase with okadaic acid-sensitivity similar to PP1. Okadaic Acid H1.0 linker histone Homo sapiens
4 Using this as a model system for the M- to G1-phase transition, we present evidence from inhibitor studies suggesting that the in vivo histone H1 phosphatase may be either PP1 or another phosphatase with similar okadaic acid-sensitivity, but not PP2A. Okadaic Acid H1.0 linker histone Homo sapiens