Dessev, G., Iovcheva-Dessev, C., Bischoff, J. R., Beach, D., Goldman, R. (February 1991) A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro. J Cell Biol, 112 (4). pp. 523-33. ISSN 0021-9525 (Print)0021-9525 (Linking)
Abstract
Cell-free extracts prepared from activated clam oocytes contain factors which induce phosphorylation of the single 67-kD lamin (L67), disassemble clam oocyte nuclei, and cause chromosome condensation in vitro (Dessev, G., R. Palazzo, L. Rebhun, and R. Goldman. 1989. Dev. Biol. 131:469-504). To identify these factors, we have fractionated the oocyte extracts. The nuclear lamina disassembly (NLD) activity, together with a protein kinase activity specific for L67, appear as a single peak throughout a number of purification steps. This peak also contains p34cdc2, cyclin B, and histone H1-kinase activity, which are components of the M-phase promoting factor (MPF). The NLD/L67-kinase activity is depleted by exposure of this purified material to Sepharose conjugated to p13suc1, and is restored upon addition of a p34cdc2/p62 complex from HeLa cells. The latter complex phosphorylates L67 and induces NLD in the absence of other clam oocyte proteins. Our results suggest that a single protein kinase activity (p34cdc2-H1 kinase, identical with MPF) phosphorylates the lamin and is involved in the meiotic breakdown of the nuclear envelope in clam oocytes.
Item Type: | Paper |
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Uncontrolled Keywords: | Animals Bivalvia CDC2 Protein Kinase/isolation & purification/*metabolism Cell Nucleus/*metabolism Chromosomes/physiology Cyclins/isolation & purification/*metabolism HeLa Cells Humans In Vitro Techniques Lamins Macromolecular Substances Maturation-Promoting Factor/physiology Nuclear Envelope/metabolism Nuclear Proteins/*metabolism Oocytes Phosphorylation Substrate Specificity |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > Cyclins bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2 bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation |
CSHL Authors: | |
Communities: | CSHL labs > Beach lab |
Depositing User: | Matt Covey |
Date: | February 1991 |
Date Deposited: | 13 Jan 2016 15:50 |
Last Modified: | 13 Jan 2016 15:50 |
PMCID: | PMC2288851 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/32060 |
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