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Protein phosphorylation is involved in the regulation of chromatin condensation during interphase
Author(s) -
Dombrádi Viktor,
Cohen Paricia T.W.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81402-8
Subject(s) - chromatin , premature chromosome condensation , interphase , dephosphorylation , serine , phosphatase , prophase , phosphorylation , protein phosphatase 1 , mutant , protein phosphatase 2 , biology , protein subunit , point mutation , chemistry , microbiology and biotechnology , gene , genetics , biochemistry , meiosis
Loci affecting the condensation state of interphase chromatin have been previously identified from analysis of suppression and enhancement of position effect variegation (PEV) in Drosophila . Here we show that Su‐var(3)6 and an allelic mutant, e078 , which both show suppression of PEV in the heterozygous state, have point mutations (Gly 220 →Ser and Gly 220 →Asp, respectively) in a protein phosphatase 1 catalytic subunit located at 87B (PP1 87B). The mutated glycine is conserved in all known protein serine/threonine phosphatases in the same gene family, and its substitution decreases PP1 activity. We conclude that protein dephosphorylation by PP1 87B regulates the condensation state of chromatin during interphase.