MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Other Versions of this Article:
MCB.00018-07v1
27/24/8533    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kang, T.-H.
Right arrow Articles by Kim, K.-T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kang, T.-H.
Right arrow Articles by Kim, K.-T.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, December 2007, p. 8533-8546, Vol. 27, No. 24
0270-7306/07/$08.00+0     doi:10.1128/MCB.00018-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Mitotic Histone H3 Phosphorylation by Vaccinia-Related Kinase 1 in Mammalian Cells{triangledown} ,{dagger}

Tae-Hong Kang,1 Do-Young Park,1 Yoon Ha Choi,1 Kyung-Jin Kim,2 Ho Sup Yoon,3 and Kyong-Tai Kim1*

Department of Life Science, Division of Molecular & Life Science, Pohang University of Science and Technology (POSTECH), San-31, Hyoja-Dong, Pohang 790-784, Republic of Korea,1 X-Ray Research Group, Pohang Accelerator Laboratory, Pohang 790-784, Republic of Korea,2 Division of Structural and Computational Biology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore3

Received 4 January 2007/ Returned for modification 13 March 2007/ Accepted 25 September 2007

Mitotic chromatin condensation is essential for cell division in eukaryotes. Posttranslational modification of the N-terminal tail of histone proteins, particularly by phosphorylation by mitotic histone kinases, may facilitate this process. In mammals, aurora B is believed to be the mitotic histone H3 Ser10 kinase; however, it is not sufficient to phosphorylate H3 Ser10 with aurora B alone. We show that histone H3 is phosphorylated by vaccinia-related kinase 1 (VRK1). Direct phosphorylation of Thr3 and Ser10 in H3 by VRK1 both in vitro and in vivo was observed. Loss of VRK1 activity was associated with a marked decrease in H3 phosphorylation during mitosis. Phosphorylation of Ser10 by VRK1 is similar to that by aurora B. Moreover, expression and chromatin localization of VRK1 depended on the cell cycle phase. Overexpression of VRK1 resulted in a dramatic condensation of nuclei. Our findings collectively support a role of VRK1 as a novel mitotic histone H3 kinase in mammals.


* Corresponding author. Mailing address: Department of Life Science, Division of Molecular & Life Science, Pohang University of Science and Technology (POSTECH), San-31, Hyoja-Dong, Pohang 790-784, Republic of Korea. Phone: 82 54 279 2297. Fax: 82 54 279 2199. E-mail: ktk{at}postech.ac.kr

{triangledown} Published ahead of print on 15 October 2007.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.


Molecular and Cellular Biology, December 2007, p. 8533-8546, Vol. 27, No. 24
0270-7306/07/$08.00+0     doi:10.1128/MCB.00018-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2007 by the American Society for Microbiology. All rights reserved.