The chaperone like function of the nonhistone protein HMGB1

Biochemical and Biophysical Research Communications

Volumn 432, Issue 2, 2013, Pages 231-235

  Osmanov, Taner ^a   Ugrinova, Iva ^a   Pasheva, Evdokia ^a  

^a BULGARIAN ACADEMY OF SCIENCES   (Bulgaria)

Author keywords

Acetylation; Chaperone; HMGB1 protein; Nucleosome reconstitution

Indexed keywords

CHAPERONE; HIGH MOBILITY GROUP B1 PROTEIN; SODIUM CHLORIDE;

ARTICLE; DIALYSIS; DNA STRUCTURE; NUCLEOSOME; PRIORITY JOURNAL;

ANIMALS; DNA; HMGB1 PROTEIN; MOLECULAR CHAPERONES; NUCLEIC ACID CONFORMATION; NUCLEOSOMES;

EID: 84875268365     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.02.008     Document Type: Article

References (32)

1. Laskey R.A., Honda B.M., Mills A.D., Finch J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 1978, 275:416-420.
2. Jorcano J.L., Ruiz-Carrillo A. H3.H4 tetramer directs DNA and core histone octamer assembly in the nucleosome core particle. Biochemistry 1979, 18:768-774.
3. Haushalter K.A., Kadonaga J.T. Chromatin assembly by DNA-translocating motors. Nat. Rev. Mol. Cell Biol. 2003, 4:613-620.
4. Ransom M., Dennehey B.K., Tyler J.K. Chaperoning histones during DNA replication and repair. Cell 2010, 140:183-195.
5. Bianchi M.E., Bertrame M., Paonessa G. Specific recognition of cruciform DNA by nuclear protein HMG1. Science 1989, 243:1056-1059.
6. Pil P.M., Lippard S.J. Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science 1992, 256:234-237.
7. Hughes E.N., Engelsberg B.N., Billings P.C. Purification of nuclear proteins that bind to cisplatin-damaged DNA. Identity with high mobility group proteins 1 and 2. J. Biol. Chem. 1992, 267:13520-13527.
8. Pasheva E.A., Pashev I.G., Favre A. Preferential binding of high mobility group 1 protein to UV-damaged DNA. Role of the COOH-terminal domain. J. Biol. Chem. 1998, 273:24730-24736.
9. Gaillard C., Strauss F. High affinity binding of proteins HMG1 and HMG2 to semicatenated DNA loops. BMC Mol. Biol. 2000, 1:1.
10. Pil P.M., Chow C.S., Lippard S.J. High-mobility-group 1 protein mediates DNA bending as determined by ring closures. Proc. Natl. Acad. Sci. USA 1993, 90:9465-9469.
11. Paul T.T., Hakynson M.J., Johnson R.C. The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures. Genes Dev. 1993, 7:1521-1534.
12. Onate S.A., Prendergast P., Wagner J.P., Nissen M., Reeves R., Pettijohn D.E., Edwards D.P. The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences. Mol. Cell Biol. 1994, 14:3376-3391.
13. Sheflin L.G., Spaulding S.W. High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA. Biochemistry 1989, 28:5658-5664.
14. Stros M., Storkova J., Thomas J. DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain. Nucleic Acids Res. 1994, 22:1044-1051.
15. Ugrinova I., Pashev I.G., Pasheva E.A. Post-synthetic acetylation of HMGB1 protein modulates its interactions with supercoiled DNA. Mol. Biol. Rep. 2009, 36:1399-1404.
16. Ugrinova I., Pasheva E., Armengaud J., et al. In vivo acetylation of HMGB1 protein enhances its binding affinity to distorted DNA structures. Biochemistry 2001, 40:14655-14660.
17. Ugrinova I., Mitkova E., Moskalenko C., et al. The DNA bending versus DNA end-joining activity of HMGB1 protein is modulated in vitro by acetylation. Biochemistry 2007, 46:2111-2117.
18. Lowary P.T., Widom J. New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol. 1998, 276:19-42.
19. Luger K., Rechsteiner T.J., Richmond T.J. Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol. Biol. 1999, 119:1-16.
20. Angelov D., Bondarenko V.A., Almagro S., Menoni H., Mongélard F., Hans F., Mietton F., Studitsky V.M., Hamiche A., Dimitrov S., Bouvet P. Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes. EMBO J. 2006, 25:1669-1679.
21. Van Holde K. Chromatin 1988, Springer Verlag KG, Berlin.
22. Tsanev R., Russev G., Pashev I., Zlatanova J. Replication and Transcription of Chromatin 1992, CRC Press Inc., Boca Raton, FL.
23. Ito T., Bulger M., Kobayashi R., Kadonaga J.T. Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays. Mol. Cell Biol. 1996, 16:3112-3124.
24. Das C., Tyler J.K., Churchill M.E. The histone shuffle: histone chaperones in an energetic dance. Trends Biochem. Sci. 2010, 35:476-489.
25. Eitoku M., Sato L., Senda T., Horikoshi M. Histone chaperones: 30 years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly. Cell. Mol. Life Sci. 2008, 65:414-444.
26. Winkler D.D., Luger K. The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization. J. Biol. Chem. 2011, 286:18369-18374.
27. Luk E., Vu N.D., Patteson K., Mizuguchi G., Wu W.H., Ranjan A., Backus J., Sen S., Lewis M., Bai Y., Wu C. Chz1, a nuclear chaperone for histone H2AZ. Mol. Cell 2007, 25:357-368.
28. Straube K., Blackwell J.S., Pemberton L.F. Nap1 and Chz1 have separate Htz1 nuclear import and assembly functions. Traffic 2010, 11:185-197.
29. Mosammaparast N., Ewart C.S., Pemberton L.F. A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J. 2002, 21:6527-6538.
30. Bowman G.D. Mechanisms of ATP-dependent nucleosome sliding. Curr. Opin. Struct. Biol. 2010, 20:73-81.
31. Ugrinova I., Pashev I.G., Pasheva E.A. Nucleosome binding properties and co-remodeling activities of native and in vivo acetylated HMGB-1 and HMGB-2 proteins. Biochemistry 2009, 48:6502-6507.
32. Bonaldi T., Langst G., Strohner R., Becker P.B., Bianchi M.E. The DNA chaperone HMGB1 facilitates ACF/CHRAC dependent nucleosome sliding. EMBO J. 2002, 21:6865-6873.