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. 2007 Jun 29;64(19-20):2590. doi: 10.1007/s00018-007-7162-3

The HMG-box: a versatile protein domain occurring in a wide variety of DNA-binding proteins

M Štros 1,, D Launholt 2, K D Grasser 2,
PMCID: PMC11136187  PMID: 17599239

Abstract.

The HMG-box domain of ~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.

Keywords. High-mobility group (HMG) protein, DNA binding, chromatin, architectural factor, transcription factor, genomic stability, human and plant genome

Footnotes

Received 30 March 2007; received after revision 29 May 2007; accepted 18 June 2007

Contributor Information

M. Štros, Email: stros@ibp.cz

K. D. Grasser, Email: kdg@bio.aau.dk


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

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