Nucleic Acids Research, 2003, Vol. 31, No. 3 878-885
© 2003 Oxford University Press
Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase
Institute of Genetics, University of Bonn, Roemerstrasse 164, D-53117 Bonn, Germany
*To whom correspondence should be addressed. Tel: +49 228 734 258; Fax: +49 228 734 263; Email: kh.scheidtmann{at}uni-bonn.de
Death-associated protein (DAP)-like kinase (Dlk), also known as Zipper interacting protein (ZIP) kinase, is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. It interacts with transcription and splicing factors as well as with pro-apoptotic protein Par-4 suggesting that it participates in multiple cellular processes. To explore the significance of histone phosphorylation by Dlk, we determined the phosphorylation site in H3 and generated phosphospecific antibodies for in vivo analyses. Interestingly, Dlk/ZIP kinase phosphorylated histone H3 at a novel site, Thr11, rather than Ser10, which is characteristic of mitotic chromosomes. Immunoblotting and confocal immunofluorescence analyses demonstrated that phosphoryl ation of H3 at Thr11 occurred in vivo and was restricted to mitosis as well. It was discernable from prophase to early anaphase and particularly enriched at centromeres. Strikingly, during this time interval, Dlk was associated with centromeres too, as revealed by stable expression of a green fluorescent protein (GFP)-Dlk fusion protein. These findings strongly suggest that Dlk is a centromere-specific histone kinase that might play a role in labeling centromere-specific chromatin for subsequent mitotic processes.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  J. Low, S. Huang, W. Blosser, M. Dowless, J. Burch, B. Neubauer, and L. Stancato High-content imaging characterization of cell cycle therapeutics through in vitro and in vivo subpopulation analysis Mol. Cancer Ther., August 1, 2008; 7(8): 2455 - 2463. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Eberlin, C. Grauffel, M. Oulad-Abdelghani, F. Robert, M.-E. Torres-Padilla, R. Lambrot, D. Spehner, L. Ponce-Perez, J.-M. Wurtz, R. H. Stote, et al. Histone H3 Tails Containing Dimethylated Lysine and Adjacent Phosphorylated Serine Modifications Adopt a Specific Conformation during Mitosis and Meiosis Mol. Cell. Biol., March 1, 2008; 28(5): 1739 - 1754. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T.-H. Kang, D.-Y. Park, Y. H. Choi, K.-J. Kim, H. S. Yoon, and K.-T. Kim Mitotic Histone H3 Phosphorylation by Vaccinia-Related Kinase 1 in Mammalian Cells Mol. Cell. Biol., December 15, 2007; 27(24): 8533 - 8546. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Bonenfant, H. Towbin, M. Coulot, P. Schindler, D. R. Mueller, and J. van Oostrum Analysis of Dynamic Changes in Post-translational Modifications of Human Histones during Cell Cycle by Mass Spectrometry Mol. Cell. Proteomics, November 1, 2007; 6(11): 1917 - 1932. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Ito Role of Histone Modification in Chromatin Dynamics J. Biochem., May 1, 2007; 141(5): 609 - 614. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Krishnamoorthy, X. Chen, J. Govin, W. L. Cheung, J. Dorsey, K. Schindler, E. Winter, C. D. Allis, V. Guacci, S. Khochbin, et al. Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is conserved in fly and mouse spermatogenesis Genes & Dev., September 15, 2006; 20(18): 2580 - 2592. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. B. Hake, B. A. Garcia, M. Kauer, S. P. Baker, J. Shabanowitz, D. F. Hunt, and C. D. Allis Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes PNAS, May 3, 2005; 102(18): 6344 - 6349. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. M. Bode and Z. Dong Inducible Covalent Posttranslational Modification of Histone H3 Sci. Signal., April 26, 2005; 2005(281): re4 - re4. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Demidov, D. Van Damme, D. Geelen, F. R. Blattner, and A. Houben Identification and Dynamics of Two Classes of Aurora-Like Kinases in Arabidopsis and Other Plants PLANT CELL, March 1, 2005; 17(3): 836 - 848. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Dai, S. Sultan, S. S. Taylor, and J. M.G. Higgins The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment Genes & Dev., February 15, 2005; 19(4): 472 - 488. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
X. Zhang, X. Li, J. B. Marshall, C. X. Zhong, and R. K. Dawe Phosphoserines on Maize CENTROMERIC HISTONE H3 and Histone H3 Demarcate the Centromere and Pericentromere during Chromosome Segregation PLANT CELL, February 1, 2005; 17(2): 572 - 583. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Shani, L. Marash, D. Gozuacik, S. Bialik, L. Teitelbaum, G. Shohat, and A. Kimchi Death-Associated Protein Kinase Phosphorylates ZIP Kinase, Forming a Unique Kinase Hierarchy To Activate Its Cell Death Functions Mol. Cell. Biol., October 1, 2004; 24(19): 8611 - 8626. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Burgdorf, P. Leister, and K. H. Scheidtmann TSG101 Interacts with Apoptosis-antagonizing Transcription Factor and Enhances Androgen Receptor-mediated Transcription by Promoting Its Monoubiquitination J. Biol. Chem., April 23, 2004; 279(17): 17524 - 17534. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. A. Borkovich, L. A. Alex, O. Yarden, M. Freitag, G. E. Turner, N. D. Read, S. Seiler, D. Bell-Pedersen, J. Paietta, N. Plesofsky, et al. Lessons from the Genome Sequence of Neurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism Microbiol. Mol. Biol. Rev., March 1, 2004; 68(1): 1 - 108. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. J. Nowak, C.-Y. Pai, and V. G. Corces Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster Mol. Cell. Biol., September 1, 2003; 23(17): 6129 - 6138. [Abstract] [Full Text] [PDF]
|
|