| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print June 13, 2002
J. Biol. Chem, 10.1074/jbc.M203814200
Submitted on April 19, 2002
Revised on June 12, 2002
Accepted on June 12, 2002
Department of Biotechnology, Aalborg University, Aalborg DK-9000
Corresponding Author: kdg{at}bio.auc.dk
The high mobility group (HMG) proteins of the HMGB family are chromatin-associated proteins that can contribute to transcriptional control by interaction with certain transcription factors. Using the transcription factor Dof2 and five different maize HMGB proteins, we have examined the specificity of the HMGB-transcription factor interaction. The HMG-box DNA binding domain of HMGB1 is sufficient for the interaction with Dof2. Although all tested HMGB proteins can interact with Dof2, the various HMGB proteins stimulate the binding of Dof2 to its DNA target site with different efficiencies. The HMGB5 protein is clearly the most potent facilitator of Dof2 DNA binding. Maximal stimulation of the DNA binding by the HMGB proteins requires association of HMGB and Dof2 prior to DNA binding. HMGB5 and Dof2 form a ternary complex with the DNA, but within the protein/DNA-complex the interaction of HMGB5 and Dof2 is different from that in solution, as in contrast to the proteins in solution, they cannot be crosslinked with glutaraldehyde when bound to DNA. Phosphorylation of HMGB1 by protein kinase CK2 abolishes the interaction with Dof2 and the stimulation of Dof2 DNA binding. These findings indicate that transcription factors may recruit certain members of the HMGB family as assistant factors.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  K. J. Kwak, J. Y. Kim, Y. O. Kim, and H. Kang Characterization of Transgenic Arabidopsis Plants Overexpressing High Mobility Group B Proteins under High Salinity, Drought or Cold Stress Plant Cell Physiol., February 1, 2007; 48(2): 221 - 231. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Samaniego, S. Y. Jeong, C. de la Torre, I. Meier, and S. M. Diaz de la Espina CK2 phosphorylation weakens 90 kDa MFP1 association to the nuclear matrix in Allium cepa J. Exp. Bot., January 1, 2006; 57(1): 113 - 124. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Yanagisawa Dof Domain Proteins: Plant-Specific Transcription Factors Associated with Diverse Phenomena Unique to Plants Plant Cell Physiol., April 15, 2004; 45(4): 386 - 391. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Barz, K. Ackermann, G. Dubois, R. Eils, and W. Pyerin Genome-wide expression screens indicate a global role for protein kinase CK2 in chromatin remodeling J. Cell Sci., April 15, 2003; 116(8): 1563 - 1577. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
