HMGB1 and HMGB2 are part of the chromatin non-histone high mobility group proteins 1 and 2. These proteins (containing multiple HMG-boxes) are conserved domains of 80 amino acids which mediate the DNA binding of many proteins. HMG box domains recognize DNA structure. Both HMGB1 and HMGB2 contain an N-terminal HMG box, a central HMG box, and an acidic carboxy terminus. The acidic tails of these proteins contain multiple serine residues which match the phosphorylation consensus sites of casein kinase II, and phosphorylation of this domain appears to be important for proper functioning of these proteins. HMGB1 and HMGB2 have been shown to facilitate the binding of various sequence-specific transcription factors to their respective DNA binding sites. They may also serve as architectural factors that recognize and mediate DNA structural changes that accompany various events such as DNA repair, transcription, and replication.
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HEK293T cells were transfected with the pCMV6-ENTRY control or pCMV6-ENTRY HMGB1 (RC205918) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-HMGB1.