HMG1 and 2: architectural DNA-binding proteins - PubMed (original) (raw)
Review
. 2001 Aug;29(Pt 4):395-401.
doi: 10.1042/bst0290395.
Affiliations
- PMID: 11497996
- DOI: 10.1042/bst0290395
Review
HMG1 and 2: architectural DNA-binding proteins
J O Thomas. Biochem Soc Trans. 2001 Aug.
Abstract
HMG1 and 2 (high mobility group proteins 1 and 2; renamed HMGB1 and 2) contain two DNA-binding HMG-box domains (A and B) and a long acidic C-terminal domain. They bind DNA without sequence specificity, but have a high affinity for bent or distorted DNA, and bend linear DNA. The individual A and B boxes (which, although broadly similar, show both structural and functional differences) exhibit many of the structure-specific properties of the whole protein. The acidic tail modulates the affinity of the tandem HMG boxes in HMG1 and 2 for a variety of DNA targets, including four-way junctions, but not distorted DNA minicircles, to which the proteins bind with very high affinity. HMG1 and 2 appear to play important architectural roles in the assembly of nucleoprotein complexes in a variety of biological processes, for example V(D)J recombination, the initiation of transcription, and DNA repair.
Similar articles
- Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA.
Stros M, Reich J. Stros M, et al. Eur J Biochem. 1998 Jan 15;251(1-2):427-34. doi: 10.1046/j.1432-1327.1998.2510427.x. Eur J Biochem. 1998. PMID: 9492314 - Structural requirements for cooperative binding of HMG1 to DNA minicircles.
Webb M, Payet D, Lee KB, Travers AA, Thomas JO. Webb M, et al. J Mol Biol. 2001 May 25;309(1):79-88. doi: 10.1006/jmbi.2001.4667. J Mol Biol. 2001. PMID: 11491303 - HMG1 and 2, and related 'architectural' DNA-binding proteins.
Thomas JO, Travers AA. Thomas JO, et al. Trends Biochem Sci. 2001 Mar;26(3):167-74. doi: 10.1016/s0968-0004(01)01801-1. Trends Biochem Sci. 2001. PMID: 11246022 Review. - The bounty of RAGs: recombination signal complexes and reaction outcomes.
Swanson PC. Swanson PC. Immunol Rev. 2004 Aug;200:90-114. doi: 10.1111/j.0105-2896.2004.00159.x. Immunol Rev. 2004. PMID: 15242399 Review.
Cited by
- Diflunisal targets the HMGB1/CXCL12 heterocomplex and blocks immune cell recruitment.
De Leo F, Quilici G, Tirone M, De Marchis F, Mannella V, Zucchelli C, Preti A, Gori A, Casalgrandi M, Mezzapelle R, Bianchi ME, Musco G. De Leo F, et al. EMBO Rep. 2019 Oct 4;20(10):e47788. doi: 10.15252/embr.201947788. Epub 2019 Aug 14. EMBO Rep. 2019. PMID: 31418171 Free PMC article. - A poxvirus host range protein, CP77, binds to a cellular protein, HMG20A, and regulates its dissociation from the vaccinia virus genome in CHO-K1 cells.
Hsiao JC, Chao CC, Young MJ, Chang YT, Cho EC, Chang W. Hsiao JC, et al. J Virol. 2006 Aug;80(15):7714-28. doi: 10.1128/JVI.00207-06. J Virol. 2006. PMID: 16840350 Free PMC article. - High-mobility group box 1, oxidative stress, and disease.
Tang D, Kang R, Zeh HJ 3rd, Lotze MT. Tang D, et al. Antioxid Redox Signal. 2011 Apr 1;14(7):1315-35. doi: 10.1089/ars.2010.3356. Antioxid Redox Signal. 2011. PMID: 20969478 Free PMC article. Review. - Dominance and Epistasis Interactions Revealed as Important Variants for Leaf Traits of Maize NAM Population.
Monir MM, Zhu J. Monir MM, et al. Front Plant Sci. 2018 Jun 18;9:627. doi: 10.3389/fpls.2018.00627. eCollection 2018. Front Plant Sci. 2018. PMID: 29967625 Free PMC article. - Members of the high mobility group B protein family are dynamically expressed in embryonic neural stem cells.
Abraham AB, Bronstein R, Chen EI, Koller A, Ronfani L, Maletic-Savatic M, Tsirka SE. Abraham AB, et al. Proteome Sci. 2013 Apr 27;11(1):18. doi: 10.1186/1477-5956-11-18. Proteome Sci. 2013. PMID: 23621913 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases