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Activation of p34cdc2 kinase by cyclin A

Functional clam cyclin A and B proteins have been produced using a baculovirus expression system. Both cyclin A and B can induce meiosis I and meiosis II in Xenopus in the absence of protein synthesis. Half- maximal induction occurs at 50 nM for cyclin A and 250 nM for cyclin B. Addition of 25 nM cy...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1991
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2288969/
https://www.ncbi.nlm.nih.gov/pubmed/1826688
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description Functional clam cyclin A and B proteins have been produced using a baculovirus expression system. Both cyclin A and B can induce meiosis I and meiosis II in Xenopus in the absence of protein synthesis. Half- maximal induction occurs at 50 nM for cyclin A and 250 nM for cyclin B. Addition of 25 nM cyclin A to activated Xenopus egg extracts arrested in the cell cycle by treatment with RNase or emetine activates cdc2 kinase to the normal metaphase level and stimulates one oscillatory cell cycle. High levels of cyclin A cause marked hyperactivation of cdc2 kinase and a stable arrest at the metaphase point in the cell cycle. Kinetic studies demonstrate the concentration of cyclin A added does not affect the 10 min lag period required for kinase activation or the timing of maximal activity, but does control the rate of deactivation of cdc2 kinase during exit from mitosis. In addition, exogenous clam cyclin A inhibits the degradation of both A- and B-type endogenous Xenopus cyclins. These results define a system for investigating the biochemistry and regulation of cdc2 kinase activation by cyclin A.
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spelling pubmed-22889692008-05-01 Activation of p34cdc2 kinase by cyclin A J Cell Biol Articles Functional clam cyclin A and B proteins have been produced using a baculovirus expression system. Both cyclin A and B can induce meiosis I and meiosis II in Xenopus in the absence of protein synthesis. Half- maximal induction occurs at 50 nM for cyclin A and 250 nM for cyclin B. Addition of 25 nM cyclin A to activated Xenopus egg extracts arrested in the cell cycle by treatment with RNase or emetine activates cdc2 kinase to the normal metaphase level and stimulates one oscillatory cell cycle. High levels of cyclin A cause marked hyperactivation of cdc2 kinase and a stable arrest at the metaphase point in the cell cycle. Kinetic studies demonstrate the concentration of cyclin A added does not affect the 10 min lag period required for kinase activation or the timing of maximal activity, but does control the rate of deactivation of cdc2 kinase during exit from mitosis. In addition, exogenous clam cyclin A inhibits the degradation of both A- and B-type endogenous Xenopus cyclins. These results define a system for investigating the biochemistry and regulation of cdc2 kinase activation by cyclin A. The Rockefeller University Press 1991-05-01 /pmc/articles/PMC2288969/ /pubmed/1826688 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Activation of p34cdc2 kinase by cyclin A
title Activation of p34cdc2 kinase by cyclin A
title_full Activation of p34cdc2 kinase by cyclin A
title_fullStr Activation of p34cdc2 kinase by cyclin A
title_full_unstemmed Activation of p34cdc2 kinase by cyclin A
title_short Activation of p34cdc2 kinase by cyclin A
title_sort activation of p34cdc2 kinase by cyclin a
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2288969/
https://www.ncbi.nlm.nih.gov/pubmed/1826688