Abstract
Various types of proteins are required for nuclear organization, which confers a variety of nuclear functions in eukaryotic cells. A set of proteins forms the chromosomal backbone (Paulson and Laemmli 1977) and different sets of proteins including chromatin-remodeling factors regulate the utilization of genetic code in chromosomal DNA (Boulikas 1995; Moazed 2001; Muchardt and Yaniv 2001). Eukaryotic chromosomes are topologically attached to the nuclear matrix (NM) or scaffold, a network of protein fibers referred to as the skeletal framework of the nucleus. The NM or scaffold is operationally defined as the residual structures that remain insoluble after extraction of nuclei with a high concentration of either salt or detergent. Several members of the group of proteins classified as components of the NM can directly bind to particular segments of chromosomal DNA. A DNA segment to which matrix and scaffold proteins can bind is termed a matrix or scaffold attachment region (MAR/SAR) (Cockerill and Garrard 1986; Gasser and Laemmli 1986; Cockerill et al. 1987; Jarman and Higgs 1988). One significant role of MAR/SARs that was revealed by structural analyses of the nucleus and chromosomes is the matrix- or scaffold-mediated stabilization of chromosomal structure. Chromosomal loops with an approximate length of ∼60 kilobases yield compact configurations of chromosomes.
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References
Alvarez JD, Yasui DH, Niida H, Joh T, Loh DY, Kohwi-Shigematsu T (2000) The MAR-binding protein SATB1 orchestrates temporal and spatial expression of multiple genes during T-cell development. Genes Dev 14:521–535
Boulikas T (1995) Chromatin domains and prediction of MAR sequences. Int Rev Cytol 162A:279–388
Boyes J, Bird A (1991) DNA methylation inhibits transcription indirectly via a methyl-CpG binding protein. Cell 64:1123–1134
Cai S, Han H-J, Kohwi-Shigematsu T (2003) Tissue-specific nuclear architecture and gene expression regulated by SATB1. Nat Genet 34:42–51
Chesnokov IN, Schmid CW (1995) Specific Alu binding protein from human sperm chromatin prevents DNA methylation. J Biol Chem 270:18539–18542
Cockerill PN, Garrard WT (1986) Chromosomal loop anchorage of the kappa immunoglobulin gene occurs next to the enhancer in a region containing topoisomerase II sites. Cell 44:273–282
Cockerill PN, Yuen M-H, Garrard WT (1987) The enhancer of the immunoglobulin heavy chain locus is flanked by presumptive chromosomal loop anchorage elements. J Biol Chem 262:5394–5497
Dickinson LA, Joh T, Kohwi Y, Kohwi-Shigematsu T (1992) A tissue-specific MAR/SAR DNA-binding protein with unusual binding site recognition. Cell 70:631–645
Fackelmayer FO, Dahm K, Renz A, Ramsperger U, Richter A (1994) Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro. Eur J Biochem 221:749–757
Forrester WC, van Genderen C, Jenuwein T, Grosschedl R (1994) Dependence of enhancer-mediated transcription of the immunoglobulin mu gene on nuclear matrix attachment regions. Science 265:1221–1225
Fuks, F, Hurd PJ, Wolf D, Nan X, Bird AP, Kouzarides T (2003) The methyl-CpG-binding protein MeCP2 links DNA methylation to histone methylation. J Biol Chem 278:4035–4040
Gasser SM, Laemmli UK (1986) Cohabitation of scaffold binding regions with upstream/enhancer elements of three developmentally regulated genes of D. melanogaster. Cell 46:521–530
Hagerman P J (1990) Sequence-directed curvature of DNA. Annu Rev Biochem 59:775–781
Hibino Y, Nakamura K, Tsukada S, Sugano N (1993) Purification and characterization of nuclear scaffold proteins which bind to a highly repetitive bent DNA from rat liver. Biochim Biophys Acta 1174:162–170
Hibino Y, Ohzeki H, Hirose N, Morita Y, Sugano N (1998a) Involvement of DNA methylation in binding of a highly repetitive DNA component to nuclear scaffold proteins from rat liver. Biochem Biophys Res Commun 252:296–301
Hibino Y, Ohzeki H, Hirose N, Sugano N (1998b) Involvement of phosphorylation in binding of nuclear scaffold proteins from rat liver to a highly repetitive DNA component. Biochim Biophys Acta 1396:88–96
Hibino Y, Ohzeki H, Sugano N, Hiraga K (2000) Transcription modulation by a rat nuclear scaffold protein, P130, and a rat highly repetitive DNA component or various types of animal and plant matrix or scaffold attachment regions. Biochem Biophys Res Commun 279:282–287
Ikeda Y, Nakamura K, Iwakami N, Hibino Y, Sugano N (1990) Base sequences of highly repetitive components in nuclear DNAs from rat liver and rat-ascites hepatoma. Cancer Lett 55:201–208
Jarman AP, Higgs DR (1988) Nuclear scaffold attachment sites in the human globin gene complexes. EMBO J 7:3337–3344
Jenuwein T, Forrester WC, Fernández-Herrero LA, Laible G, Dull M, Grosschedl R (1997) Extension of chromatin accessibility by nuclear matrix attachment regions. Nature 385:269–272
Kohwi-Shigematsu T, Maass K, Bode J (1997) A thymocyte factor SATB1 suppresses transcription of stably integrated matrix-attachment region-linked reporter genes. Biochemistry 36:12005–12010
Li W, Chen HY, Davie JR (1996) Properties of chicken erythrocyte histone deacetylase associated with the nuclear matrix. Biochem J 314:631–637
Ma H, Siegel AJ, Berezney R (1999) Association of chromosome territories with the nuclear matrix: disruption of human chromosome territories correlates with the release of a subset of nuclear matrix proteins. J Cell Biol 146:531–542
Martínez-Balbás A, Rodríguez-Campos A, García-Ramírez M, Sainz J, Carrera P, Aymamí J, Azorín F (1990) Satellite DNAs contain sequences that induce curvature. Biochemistry 29:2342–2348
Moazed D (2001) Common themes in mechanisms of gene silencing. Mol Cell 8:489–498
Muchardt C, Yaniv M (2001) When the SWI/SNF complex remodels.the cell cycle. Oncogene 20:3067–3075
Nan X, Campoy FJ, Bird A (1997) MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin. Cell 88:471–481
Nan X, Ng H-H, Johnson CA, Laherty CD, Turner BM, Eisenman RN, Bird A (1998) Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393:386–389
Nayler O, Strätling W, Bourquin JP, Stagljar I, Lindemann L, Jasper H, Hartmann AM, Fackelmayer FO, Ullrich A, Stamm S (1998) SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements. Nucleic Acids Res 26:3542–3549
Paulson JR, Laemmli UK (1977) The structure of histone-depleted metaphase chromosomes. Cell 12:817–828
Poljak L, Seum C, Mattioni T, Laemmli UK (1994) SARs stimulate but do not confer position independent gene expression. Nucleic Acids Res 22:4386–4394
Radic MZ, Lundgren K, Hamkalo BA (1987) Curvature of mouse satellite DNA and condensation of heterochromatin. Cell 50:1101–1108
Razin SV, Mantieva VL, Georgiev GP (1979) The similarity of DNA sequences remaining bound to scaffold upon nuclease treatment of interphase nuclei and metaphase chromosomes. Nucleic Acids Res 7:1713–1735
Romig H, Fackelmayer FO, Renz A, Ramsperger U, Richter A (1992) Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements. EMBO J 11:3431–3440
Shrader TE, Crothers DM (1990) Effects of DNA sequence and histone-histone interactions on nucleosome placement. J Mol Biol 216:69–84
Singer MF (1982) Highly repeated sequences in mammalian genomes. Int Rev Cytol 76:67–112
Small D, Nelkin B, Vogelstein B (1982) Nonrandom distribution of repeated DNA sequences with respect to supercoiled loops and the nuclear matrix. Proc Natl Acad Sci USA 79:5911–5915
Weitzel JM, Buhrmester H, Strätling WH (1997) Chicken MAR-binding protein ARBP is homologous to rat methyl-CpG-binding protein MeCP2. Mol Cell Biol 17:5656–5666
Xu M, Hammer RE, Blasquez VC, Jones SL, Garrard WT (1989) Immunoglobulin kappa gene expression after stable integration. II. Role of the intronic MAR and enhancer in transgenic mice. J Biol Chem 264:21190–21195
Zink D, Cremer T, Saffrich R, Fischer R, Trendelenburg MF, Ansorge W, Stelzer EH (1998) Structure and dynamics of human interphase chromosome territories in vivo. Hum Genet 102:241–251
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Hibino, Y., Usui, T., Hiraga, K. (2007). Transcriptional Modulation by Nuclear Matrix Protein P130/MAT3 Associated with MAR/SAR. In: Nagata, K., Takeyasu, K. (eds) Nuclear Dynamics. Springer, Tokyo. https://doi.org/10.1007/978-4-431-30130-1_13
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DOI: https://doi.org/10.1007/978-4-431-30130-1_13
Publisher Name: Springer, Tokyo
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