M-phase-specific histone H1 kinase in fish oocytes. Purification, components and biochemical properties
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چکیده
منابع مشابه
Histone H1 kinase activity, germinal vesicle breakdown and M phase entry in mouse oocytes.
Meiotic reinitiation of the mouse oocyte is characterized by a slow entry into metaphase I, beginning with germinal vesicle breakdown and ending with spindle formation. It is accompanied by a cascade of protein kinases and phosphatases increasing protein phosphorylation. The activation of histone H1 kinase and that of the mitogen-activated protein kinase p42 have been compared during spontaneou...
متن کاملActivation of M-phase-specific histone H1 kinase by modification of the phosphorylation of its p34cdc2 and cyclin components.
An M-phase-specific histone H1 kinase (H1K) has been described in a wide variety of eukaryotic cell types undergoing the G2/M transition in the cell division cycle. We have used p13suc1-Sepharose affinity chromatography to purify H1K to near homogeneity from matured starfish oocytes. A yield of 67% was obtained. Active H1K behaves as a 90- to 100-kD protein and appears to be constituted of equi...
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A major protein kinase independent of Ca2+, cyclic nucleotide or diacylglycerol, the activity of which becomes maximal when cells enter M phase, decreases at ana-telophase, and is low during interphase, has been purified to near homogeneity from starfish oocytes and its catalytic subunit identified as p34cdc2. M phase-promoting factor (MPF) was found to co-purify with the M phase-specific kinas...
متن کاملChemically enucleated mouse oocytes: ultrastructure and kinetics of histone H1 kinase activity.
The objective of the study was to characterize the ultrastructure changes and biochemical mechanisms underlying the expulsion of the entire chromosome complement in chemically enucleated mouse oocytes. The ultrastructural studies demonstrated that the morphology of cytoplasts produced by etoposide-cycloheximide treatment were indistinguishable from intact metaphase I and II oocytes. Moreover, p...
متن کاملHistone Kinase from Soybean Hypocotyls: PURIFICATION, PROPERTIES, AND SUBSTRATE SPECIFICITIES.
A histone-type protein kinase (EC 2.7.1.37) has been partially purified (320-fold) from the crude extracts of soybean hypocotyls by means of a combination of gel filtration and anion exchange procedures. The purified enzyme fraction is devoid of the activities of phosphoprotein phosphatase (EC 3.1.3.16), histone protease, and casein (or phosvitin)-type kinase. The soybean histone kinase uses AT...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1992
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1992.tb16810.x