A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro

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)

URL: http://www.ncbi.nlm.nih.gov/pubmed/1825210
DOI: 10.1083/jcb.112.4.523

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
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: http://repository.cshl.edu/id/eprint/32060

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