Cellular and Molecular Life Sciences

, Volume 64, Issue 19, pp 2590-2606

First online:

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

  • M. ŠtrosAffiliated withLaboratory of Analysis of Chromosomal Proteins, Academy of Sciences of the Czech Republic, Institute of Biophysics Email author 
  • , D. LaunholtAffiliated withDepartment of Life Sciences, Aalborg University
  • , K. D. GrasserAffiliated withDepartment of Life Sciences, Aalborg University Email author 

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access


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.


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