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

Review

DOI: 10.1007/s00018-007-7162-3

Cite this article as:
Štros, M., Launholt, D. & Grasser, K.D. Cell. Mol. Life Sci. (2007) 64: 2590. doi:10.1007/s00018-007-7162-3

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 

Copyright information

© Birkhäuser Verlag, Basel 2007

Authors and Affiliations

  1. 1.Laboratory of Analysis of Chromosomal Proteins, Academy of Sciences of the Czech RepublicInstitute of BiophysicsBrnoCzech Republic
  2. 2.Department of Life SciencesAalborg UniversityAalborgDenmark

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