Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 64, Issue 19-20, Pages 2590-2606Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-007-7162-3
Keywords
high-mobility group (HMG) protein; DNA binding; chromatin; architectural factor; transcription factor; genomic stability; human and plant genome
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The HMG-box domain of similar to 75 amino acid residues was originally identified as the domain that mediates the DNA-binding of chromatin-associated high-mobility group (HMG) proteins of the HMGB type. In the last few years, HMG-box domains have been found in various DNA-binding proteins including transcription factors and subunits of chromatin-remodeling complexes. HMG-box domains mediate either non-sequence-specific (e.g., HMGB-type proteins) or sequence-specific (e.g., transcription factors) DNA binding. Both types of HMG-box domains bind non-B-type DNA structures (bent, kinked and unwound) with high affinity. In addition, HMG-box domains are involved in a variety of protein-protein interactions. Here, we have examined the human and plant genomes for genes encoding HMG-box domains. Compared to plants, human cells contain a larger variety of HMG-box proteins. Whereas in humans transcription factors are the most divergent group of HMG-box proteins, in plants the chromosomal HMGB-type proteins are most variable.
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