High-mobility group

High-Mobility Group or HMG is a group of chromosomal proteins that are involved in the regulation of DNA-dependent processes such as transcription, replication, recombination, and DNA repair.[1]

Families

The HMG proteins are subdivided into 3 superfamilies each containing a characteristic functional domain:

Proteins containing any of these embedded in their sequence are known as HMG motif proteins. HMG-box proteins are found in a variety of eukaryotic organisms.

They were originally isolated from mammalian cells, and named according to their electrophoretic mobility in polyacrylamide gels.[2]

Function

HMG proteins are thought to play a significant role in various human disorders. Disruptions and rearrangements in the genes coding for some of the HMG proteins are associated with some common benign tumors. Antibodies to HMG proteins are found in patients suffering from autoimmune diseases. The SRY gene on the Y Chromosome, responsible for male sexual differentiation, contains an HMG-Box domain. A member of the HMG family of proteins, HMGB1, has also been shown to have an extracellular activity as a chemokine, attracting neutrophils and mononuclear inflammatory cells to the infected liver.[3] The high-mobility group protein such as HMO1 [4] alters DNA architecture by binding, bending and looping. Furthermore, these HMG-box DNA-binding proteins increase the flexibility of the DNA upon binding.[5]

See also

References

  1. ↑ Rajeswari MR, Jain A (2002). "High-mobility-group chromosomal proteins, HMGA1 as potential tumour markers" (PDF). Current Science. 82 (7): 838–844.
  2. ↑ Johns EB (1982). The HMG chromosomal proteins. Boston: Academic Press. ISBN 0-12-386050-4.
  3. ↑ Sitia G, Iannacone M, Müller S, Bianchi ME, Guidotti LG (January 2007). "Treatment with HMGB1 inhibitors diminishes CTL-induced liver disease in HBV transgenic mice". J. Leukoc. Biol. 81 (1): 100–7. PMID 16935945. doi:10.1189/jlb.0306173.
  4. ↑ D. Murugesapillai et al, DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin, Nucl Acids Res (2014) 42 (14): 8996-9004
  5. ↑ D. Murugesapillai et al, Single-molecule studies of high-mobility group B architectural DNA bending proteins, Biophys Rev (2016) doi:10.1007/s12551-016-0236-4


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