spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Paulson, J. R.
Right arrow Articles by Mesner, P. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Paulson, J. R.
Right arrow Articles by Mesner, P. W.

Journal of Cell Science, Vol 107, Issue 1 267-273, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

Okadaic acid induces dephosphorylation of histone H1 in metaphase-arrested HeLa cells

JR Paulson, WA Ciesielski, BR Schram and PW Mesner
Department of Chemistry, University of Wisconsin-Oshkosh 54901.

It is shown here that treatment of metaphase-arrested HeLa cells with okadaic acid (0.15-2.5 microM) leads to dephosphorylation of histone H1. This effect is presumably due to the specific ability of okadaic acid to inhibit protein phosphatases 1 and/or 2A, because okadaic acid tetraacetate, which is not a phosphatase inhibitor, has no effect. Dephosphorylation of H1 does not occur if okadaic acid-treated cells are simultaneously treated with 20 nM calyculin A, or if the okadaic acid concentration is 5.0 microM or greater. The mechanism behind this phenomenon is not known. However, the results suggest that the chain of events leading to histone dephosphorylation may be negatively controlled by a protein phosphatase 2A, while the phosphatase which actually dephosphorylates H1 could be a protein phosphatase 1. It remains to be determined whether the phosphatase involved here is the same enzyme as that which dephosphorylates H1 at the end of normal mitosis.


This article has been cited by other articles:


Home page
 J Exp BotHome page
J. T. Polit and A. Kazmierczak
Okadaic acid (1 {micro}M) accelerates S phase and mitosis but inhibits heterochromatin replication and metaphase-anaphase transition in Vicia faba meristem cells
J. Exp. Bot., August 1, 2007; 58(11): 2785 - 2797.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Ajiro, K. Yoda, K. Utsumi, and Y. Nishikawa
Alteration of Cell Cycle-dependent Histone Phosphorylations by Okadaic Acid. INDUCTION OF MITOSIS-SPECIFIC H3 PHOSPHORYLATION AND CHROMATIN CONDENSATION IN MAMMALIAN INTERPHASE CELLS
J. Biol. Chem., May 31, 1996; 271(22): 13197 - 13201.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
J. Paulson, J. Patzlaff, and A. Vallis
Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A
J. Cell Sci., January 6, 1996; 109(6): 1437 - 1447.
[Abstract] [PDF]


© The Company of Biologists Ltd 1994