The Control of Phosphoprotein Phosphatase by the Second‐Site Phosphorylation of a Substrate

Studies with H2B Histone as Model Substrate

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 1979 English Publisher:WileyJournal:European Journal of Biochemistry, volume 99, pages 413-417 (issn: 0014-2956, eissn: 1432-1033,

Authors: H, Usui; N, Nishimura; M, Imazu; T, Imaoka; N, Konohara; M, Takeda;

doi: 10.1111/j.1432-1033.1979.tb13270.x

pmid: 227681

The Control of Phosphoprotein Phosphatase by the Second‐Site Phosphorylation of a Substrate

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Abstract

The phosphorylation of Ser‐32, in addition to Ser‐36 of H2B histone, stimulated the rate of Pi release from Ser‐36 by the small form (Mr 31000) of pig heart phosphoprotein phosphatase both in the absence and presence of 50 mM magnesium acetate. By phosphorylation at Ser‐32, the Km value for Ser‐36 phosphate in H2B histone was increased from 0.38 μM to 1.16 μM in the absence of magnesium acetate, but not significantly changed (from 37.4 μM to 26.2 μM) in the presence of magnesium acetate. With the large form (Mr 224000) of the phosphoprotein phosphatase, however, the phosphorylation at Ser‐32 suppressed the rate of Pi release from Ser‐36 both in the absence and presence of magnesium acetate. The Km value of the large form for Ser‐36 phosphate in H2B histone was nevertheless increased by phosphorylation at Ser‐32, from 1.2μM to 5.3 μM in the presence of magnesium acetate, but not changed (from 0.26 μM to 0.23 μM) in the absence of magnesium acetate.

Related Organizations

Hiroshima University
Japan

Keywords

Histones, Kinetics, Phosphoprotein Phosphatases, Serine, Animals, Cattle, Phosphorylation

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