HMGA proteins in vivo

Drugs that specifically inactivate or cross-link HMGA proteins in vivo 

CD28 response element casein kinase 2 circular dichroism 

and Bullerdiek, J. (2001) Genes Chromosomes Cancer 30, 302-304. 

(1986) Purification and Characterization of the High Mobility Group Nonhistone Chromatin Proteins. Ph.D. Thesis, pp. 1-134. Washington State University, Pullman, WA 99164. Palvimo, J. and Linnala-Kankkunen, A. (1989) FEBS Lett. 257, 101-104. 

Edberg, D.D., Adkins, J., Springer, D., and Reeves, R. (2002) Unpublished data. 

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Recent advances in mass spectrometry (MS) technology have provided researchers with an unparalleled ability to identify the types and patterns of secondary biochemical modifications found on proteins in living cells. Matrix-assisted laser desorption/ionization-MS (MALDI-MS) analyses have shown, for example, that HMGA proteins in vivo are simultaneously subject to complex patterns of phosphorylation, acetylation and methylation and that, within the same cell type, different isoforms of these proteins can exhibit quite different modification patterns [33]. Furthermore, these in vivo modifications have been demonstrated to markedly alter the binding affinity of HMGA proteins for both DNA and chromatin substrates in vitro [33]. Nevertheless, due to their number and complexity, it has been difficult to determine the actual biological function(s) played by these biochemical modifications in living cells. 

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