Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
Tóm tắt
Từ khóa
Tài liệu tham khảo
Rice, J.C. & Allis, C.D. Histone methylation versus histone acetylation: new insights into epigenetic regulation. Curr. Opin. Cell. Biol. 13, 263–273 (2001).
Strahl, B.D. & Allis, D.C. The language of covalent histone modifications. Nature 403, 41–45 (2000).
Jeppesen, P., Mitchell, A., Turner, B. & Perry, P. Antibodies to defined histone epitopes reveal variations in chromatin conformation and underacetylation of centric heterochromatin in human metaphase chromosomes. Chromosoma 101, 322–332 (1992).
Peters, A.H. et al. Loss of the suv39h histone methyltransferases impairs Mammalian heterochromatin and genome stability. Cell 107, 323–337 (2001).
Nakayama, J., Rice, J.C., Strahl, B.D., Allis, C.D. & Grewal, S.I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110–113 (2001).
Rea, S. et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593–599 (2000).
Bannister, A.J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410, 120–124 (2001).
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116–120 (2001).
Taddei, A., Maison, C., Roche, D. & Almouzni, G. Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases. Nature Cell Biol. 3, 114–120 (2001).
Ekwall, K., Olsson, T., Turner, B.M., Cranston, G. & Allshire, R.C. Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres. Cell 91, 1021–1032 (1997).
Zhang, Y. & Reinberg, D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. 15, 2343–2360 (2001).
Cheung, P., Allis, C.D. & Sassone-Corsi, P. Signaling to chromatin through histone modifications. Cell 103, 263–271 (2000).
Kipling, D., Wilson, H.E., Mitchell, A.R., Taylor, B.A. & Cooke, H.J. Mouse centromere mapping using oligonucleotide probes that detect variants of the minor satellite. Chromosoma 103, 46–55 (1994).
Akhtar, A., Zink, D. & Becker, P.B. Chromodomains are protein-RNA interaction modules. Nature 407, 405–409 (2000).
Jones, D.O., Cowell, I.G. & Singh, P.B. Mammalian chromodomain proteins: their role in genome organisation and expression. Bioessays 22, 124–137 (2000).
Avner, P. & Heard, E. X-chromosome inactivation: counting, choice and initiation. Nature Rev. Genet. 2, 59–67 (2001).
Peters, A.H.F.M. et al. Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin. Nature Genet. 30, 77–80 (2002).
Boggs, B.A. et al. Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes. Nature Genet. 30, 73–76 (2002).
Gasser, S.M. Positions of potential: nuclear organization and gene expression. Cell 104, 639–642 (2001).
Nielsen, A.L. et al. Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. Mol. Cell 7, 729–739 (2001).
Jacobs, S.A. et al. Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3. EMBO J. 20, 5232–5241 (2001).
Aagaard, L. et al. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3- 9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 18, 1923–1938 (1999).
Kornberg, R.D., LaPointe, J.W. & Lorch, Y. Preparation of nucleosomes and chromatin. Methods Enzymol. 170, 3–14 (1989).
O'Neill, L.P. & Turner, B.M. Immunoprecipitation of chromatin. Methods Enzymol. 274, 189–197 (1996).
Brown, K.E. et al. Association of transcriptionally silent genes with Ikaros complexes at centromeric heterochromatin. Cell 91, 845–854 (1997).