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The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe

Yamano, H; Gannon, J; Hunt, T; (1996) The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe. EMBO J. , 15 (19) pp. 5268-5279.

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Abstract

A cell-free system derived from Xenopus eggs was used to identify the 'destruction box' of the Schizosaccharomyces pombe B-type cyclin, Cdc13, as residues 59-67: RHALDDVSN. Expression of indestructible Cdc13 from a regulated promoter in S.pombe blocked cells in anaphase and inhibited septation, showing that destruction of Cdc13 is necessary for exit from mitosis, but not for sister chromatid separation. In contrast, strong expression of a polypeptide comprising the N-terminal 70 residues of Cdc13, which acts as a competitive inhibitor of destruction box-mediated proteolysis, inhibited both sister chromatid separation and the destruction of Cdc13, whereas an equivalent construct with a mutated destruction box did not. Appropriately timed expression of this N-terminal fragment of Cdc13 overcame the G1 arrest seen in cdc10 mutant strains, suggesting that proteins required for the initiation of S phase are subject to destruction by the same proteolytic machinery as cyclin.

Type: Article
Title: The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe
Publisher version: http://www.ncbi.nlm.nih.gov/pubmed/8895572
Additional information: Yamano, H Gannon, J Hunt, T Research Support, Non-U.S. Gov't England The EMBO journal EMBO J. 1996 Oct 1;15(19):5268-79. A cell-free system derived from Xenopus eggs was used to identify the 'destruction box' of the Schizosaccharomyces pombe B-type cyclin, Cdc13, as residues 59-67: RHALDDVSN. Expression of indestructible Cdc13 from a regulated promoter in S.pombe blocked cells in anaphase and inhibited septation, showing that destruction of Cdc13 is necessary for exit from mitosis, but not for sister chromatid separation. In contrast, strong expression of a polypeptide comprising the N-terminal 70 residues of Cdc13, which acts as a competitive inhibitor of destruction box-mediated proteolysis, inhibited both sister chromatid separation and the destruction of Cdc13, whereas an equivalent construct with a mutated destruction box did not. Appropriately timed expression of this N-terminal fragment of Cdc13 overcame the G1 arrest seen in cdc10 mutant strains, suggesting that proteins required for the initiation of S phase are subject to destruction by the same proteolytic machinery as cyclin.
Keywords: Amino Acid Sequence Anaphase/physiology Animals CDC2 Protein Kinase/biosynthesis/*metabolism Calcium Chloride/pharmacology Cell Cycle/*physiology Cell-Free System Chromatids Cyclin B Cyclins/biosynthesis/genetics/*metabolism Mutation Ovum Peptides Protamine Kinase/metabolism Proto-Oncogene Proteins c-mos/metabolism Recombinant Fusion Proteins/metabolism S Phase/physiology Schizosaccharomyces/*cytology/enzymology Temperature Xenopus
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Wolfson Institute and Cancer Institute Administration > Cancer Institute
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Wolfson Institute and Cancer Institute Administration > Cancer Institute > Research Department of Cancer Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1305885
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