Title |
The HMG-box: a versatile protein domain occurring in a wide variety of DNA-binding proteins
|
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Published in |
Cellular and Molecular Life Sciences, June 2007
|
DOI | 10.1007/s00018-007-7162-3 |
Pubmed ID | |
Authors |
M. Štros, D. Launholt, K. D. Grasser |
Abstract |
The HMG-box domain of approximately 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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Netherlands | 1 | <1% |
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Readers by professional status | Count | As % |
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Student > Ph. D. Student | 69 | 27% |
Researcher | 38 | 15% |
Student > Bachelor | 33 | 13% |
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Student > Doctoral Student | 19 | 7% |
Other | 36 | 14% |
Unknown | 33 | 13% |
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Chemistry | 3 | 1% |
Other | 11 | 4% |
Unknown | 38 | 15% |