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HMGB proteins

Agresti A, Bianchi ME (2003) HMGB proteins and gene expression. Curr Opin Genet Dev 13 170-178... [Pg.23]

Fig. 1. HMG boxes in the abundant chromosomal HMGB proteins and in other DNA-binding proteins. Fig. 1. HMG boxes in the abundant chromosomal HMGB proteins and in other DNA-binding proteins.
The interaction of the abundant HMGB proteins with both nucleosomal particles lacking linker histones and with linker histones themselves in vitro is well documented. A soluble chromatin fraction released from mouse myeloma nuclei contained mononucleosomes associated with almost stoichiometric amounts of HMGB1,2 but lacking histone HI [81]. Nhp6ap binds directly to nucleosomal particles reconstituted with chicken histones (i.e., a single histone octamer... [Pg.113]

HMGB proteins including HMGBl ([96,97] A. Simpson and J. O. Thomas, unpublished) and HMG-D [87] can also interact directly in vitro with histone HI. The interaction of HMG-D is independent of the acidic tail (suggesting that, in this case at least, non-specific charge interactions involving the tail can be excluded) but requires aminoacids 75-100, which comprise a short linker and basic region between the HMG box and the tail [87]. [Pg.115]

In addition to a potential role of HMGB proteins in nucleosome assembly, it has recently become apparent that many chromatin remodeling complexes either contain, or can associate with, a polypeptide containing an HMG-box homologous to the HMGBl B domain (Table 2). Examples of such complexes include the BAF (a mammalian SWI/SNF related complex [106]) and the Drosophila BRM (brahma)... [Pg.115]

The postulated interaction of the acidic tail of abundant HMGB proteins with core histones might suggest possible functional differences between the two major... [Pg.117]

Fig. 4. Possible mechanism for HMGB proteins in facilitating the unwrapping of nucleosomal DNA. The model postulates that the binding of an HMGB protein at an exit/entry point for the wrapped DNA increases the accessibility of the wrapped DNA both at the exit/entry points adjacent to the bound HMGB protein and also at internal positions. Such a conformational change would facilitate the binding both of sequence-specific regulatory proteins and of remodeling complexes. Adapted from Ref. [119] with permission. Fig. 4. Possible mechanism for HMGB proteins in facilitating the unwrapping of nucleosomal DNA. The model postulates that the binding of an HMGB protein at an exit/entry point for the wrapped DNA increases the accessibility of the wrapped DNA both at the exit/entry points adjacent to the bound HMGB protein and also at internal positions. Such a conformational change would facilitate the binding both of sequence-specific regulatory proteins and of remodeling complexes. Adapted from Ref. [119] with permission.
Wong, B., Masse, J.E., Yen, Y.-M., Feigon, J., and Johnson, R.C. (2002) Binding to cisplatin-modified DNA by the Saccharomyces cerevisiae HMGB protein NHP6A. Biochemistry 41, 5404-5414. [Pg.127]

Travers, A.A. (2003) Priming the nucleosome—a role for HMGB proteins EMBO Rep. 4, 131-136. Bonaldi, T., Langst, G., Strohner, R., Becker, P.B., and Bianchi, M.E. (2002) The DNA chaperone HMGBl facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J. 21, 6865-6873. [Pg.131]

Krohn, N.M., Yanagisawa, S., and Crasser, K.D. (2002) Specificity of the stimulatory interaction between chromosomal HMGB proteins and the transcription factor Dof2 and its negative regulation by protein kinase CK2-mediated phosphorylation. J. Biol. Chem. 277, 32438-32444. [Pg.132]

Since HMGB proteins appear to impair intrinsic nucleosome mobility while at the same time enhancing enzymatically driven translocation [202] this observation is not wholly consistent with a simple unwrapping from one end of the... [Pg.441]


See other pages where HMGB proteins is mentioned: [Pg.9]    [Pg.103]    [Pg.103]    [Pg.105]    [Pg.105]    [Pg.111]    [Pg.112]    [Pg.113]    [Pg.113]    [Pg.113]    [Pg.114]    [Pg.114]    [Pg.115]    [Pg.117]    [Pg.118]    [Pg.118]    [Pg.119]    [Pg.119]    [Pg.122]    [Pg.122]    [Pg.123]    [Pg.123]    [Pg.123]    [Pg.123]    [Pg.124]    [Pg.127]    [Pg.441]    [Pg.442]    [Pg.442]    [Pg.443]    [Pg.212]    [Pg.212]    [Pg.577]   
See also in sourсe #XX -- [ Pg.441 , Pg.442 ]




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