Biopolym. Cell. 1991; 7(5):71-80.
http://dx.doi.org/10.7124/bc.0002F6
Клітинна біологія
Асоціація доменів хроматину з ядерним скелетом у клітинах асцитної карциноми Ерліха. Аналіз методом нуклеопротеїд-целіт-хроматографії
1Сьяксте Н. І., 1Будилін А. В.
  1. Інститут органічного синтезу АН Латвійської РСР
    Рига, СРСР

Abstract

Методом НПЦ-хроматографії досліджено розподіл нуклеопротеїдів різної міцності в ізольованих ядрах та ядерному матриксі. У препаратах матриксу, одержаних обробкою ядер ДНКзою І, виявлено стійкий до солі сечовини (ДНК II) та нестійкий (ДНК І) зв'язки ДНК – матрикс і фракція залишкового хроматину. Всі зв'язки стійкі до дії меркаптоетанолу, ЕДТА та низької іонної сили. ДНК II чутлива до дії нуклеази S1, для її зруйнування необхідне плавлення молекули ДНК. Рестриктази викликають деградацію ДНК II з різною ефективністю: ті, що пізнають тетрануклеотид, сильніше від атакуючих гексануклеотид, серед останніх EcoRI, PstI, PvuII більш ефективні, ніж HindIII, SalGI, ВатНІ. По сумі властивостей ДНК І та ДНК II не відповідають зв'язкам ДНК – матрикс, що виявлено другими методами.
Повний текст: (PDF, російською)

References

[1] Glazkov MV. Nucleotides in rat liver cells: sedimentation and fluorescence analysis; DNA, associated with residual nuclear structures. Mol Biol (Mosk). 1986;20(6):1682-91.
[2] Zaboĭkin MM, Moiseev VL, Shapot VS, Likhtenshteĭn AV. Identification of the stable DNA-matrix complex (type II) as a site of replication fork. Mol Biol (Mosk). 1988;22(4):1119-27.
[3] Bodnar JW. A domain model for eukaryotic DNA organization: a molecular basis for cell differentiation and chromosome evolution. J Theor Biol. 1988;132(4):479-507.
[4] Kalandadze AG, Bushara SA, Vassetzky YS Jr, Razin SV. Characterization of DNA pattern in the site of permanent attachment to the nuclear matrix located in the vicinity of replication origin. Biochem Biophys Res Commun. 1990;168(1):9-15.
[5] Marilley M, Gassend-Bonnet G. Supercoiled loop organization of genomic DNA: a close relationship between loop domains, expression units, and replicon organization in rDNA from Xenopus laevis. Exp Cell Res. 1989;180(2):475-89.
[6] Razin SV, Chernokhvostov VV, Vassetzky ES Jr, Razina MV, Georgiev GP. The distribution of tightly bound proteins along the DNA chain reflects the type of cell differentiation. Nucleic Acids Res. 1988;16(9):3617-33.
[7] Stief A, Winter DM, Strätling WH, Sippel AE. A nuclear DNA attachment element mediates elevated and position-independent gene activity. Nature. 1989;341(6240):343-5.
[8] Izaurralde E, Mirkovitch J, Laemmli UK. Interaction of DNA with nuclear scaffolds in vitro. J Mol Biol. 1988;200(1):111-25.
[9] Glazkov MV. Structural-functional organization of DNA in the interphase nucleus. Structural aspects. Mol Biol (Mosk). 1988;22(1):16-30.
[10] S'iakste NI. The role of DNA breaks in the regulation of cell proliferation, differentiation and aging. Ontogenez. 1987;18(3):229-38.
[11] S'iakste NI. Interaction of various nuclear matrix proteins with DNA. Biokhimiia. 1988;53(2):256-62.
[12] S'iakste NI, Blokhin DIu. Protein composition of DNA-matrix complexes with "strong" and "weak" types of bonds, isolated from Ehrlich ascites carcinoma cells. Biokhimiia. 1989;54(7):1217-23.
[13] S'iakste NI, Zaboĭkin MM, Erenpreĭsa EA, Likhtenshteĭn AV, Shapot VS. Analysis of cellular nucleoproteins by the nucleoprotein-celite chromatography method. III. Two types of DNA-nuclear matrix interaction. Mol Biol (Mosk). 1985;19(5):1231-41.
[14] Zaboĭkin MM, Alekhina RP, Likhtenshteĭn AV. Comparative analysis of subdomain fragments of chromatin. Mol Biol (Mosk). 1989;23(3):851-61.
[15] S'iakste NI, Budylin AV. Stability of DNA-protein interactions in chromatin fractions with different sensitivity to nucleases. Mol Gen Mikrobiol Virusol. 1988;(10):30-4.
[16] Jarman AP, Higgs DR. Nuclear scaffold attachment sites in the human globin gene complexes. EMBO J. 1988;7(11):3337-44.
[17] Pauli U, Kuenzler P, Braun R. Unusual nucleoprotein structures in the vicinity of the replication origins of the extrachromosomal rDNA of the slime mould Physarum polycephalum. Biochem Cell Biol. 1988;66(9):935–41.
[18] Mielke C, Kohwi Y, Kohwi-Shigematsu T, Bode J. Hierarchical binding of DNA fragments derived from scaffold-attached regions: correlation of properties in vitro and function in vivo. Biochemistry. 1990;29(32):7475-85.
[19] Käs E, Izaurralde E, Laemmli UK. Specific inhibition of DNA binding to nuclear scaffolds and histone H1 by distamycin. The role of oligo(dA).oligo(dT) tracts. J Mol Biol. 1989;210(3):587-99.
[20] Greenstein RJ. Constitutive attachment of murine erythroleukemia cell histone-depleted DNA loops to nuclear scaffolding is found in the beta-major but not the alpha 1-globin gene. DNA. 1988;7(9):601-7.
[21] Tsutsui K, Tsutsui K, Muller MT. The nuclear scaffold exhibits DNA-binding sites selective for supercoiled DNA. J Biol Chem. 1988;263(15):7235-41.
[22] Homberger HP. Bent DNA is a structural feature of scaffold-attached regions in Drosophila melanogaster interphase nuclei. Chromosoma. 1989;98(2):99-104.
[23] Sykes RC, Lin D, Hwang SJ, Framson PE, Chinault AC. Yeast ARS function and nuclear matrix association coincide in a short sequence from the human HPRT locus. Mol Gen Genet. 1988;212(2):301-9.
[24] S'iakste NI, Budylin AV. Changes in the interaction of DNA with chromatin and nuclear matrix proteins during digestion of nuclei with restrictases and nuclease Bal 31. Biokhimiia. 1988;53(1):54-60.
[25] S'iakste NI, Budylin AV. DNA distribution in fractions differing in the strength of association with nuclear matrix during activation of DNA endonucleases in cell nuclei and treatment with nuclease S1. Mol Gen Mikrobiol Virusol. 1990;(7):21-4.
[26] Jackson DA, Dickinson P, Cook PR. Attachment of DNA to the nucleoskeleton of HeLa cells examined using physiological conditions. Nucleic Acids Res. 1990;18(15):4385-93.
[27] Werner D, Neuer-Nitsche B. Site-specific location of covalent DNA-polypeptide complexes in the chicken genome. Nucleic Acids Res. 1989;17(15):6005-15.
[28] Sjakste NI, Sjakste TG. Heterogeneity in strength bind to DNA proteins resistant to deproteinization. Bull Exp Biol Med. 1990; 110(8):194-196.
[29] Sjakste NI, Budylin AV, Sjakste TG. Disconnection of DNA domains in quiescent and differentiating cells. Nuclear structure and function. New York, 1990:365-369.
[30] Ascoli CA, Link MR, Venturo N, Kuchler RJ, Mandeles S. Identification of a rosette-enriched chromatin fraction from mouse fibroblast nuclei. Arch Biochem Biophys. 1988;263(2):334-48.
[31] Rzeszowska-Wolny J, Razin S, Puvion E, Moreau J, Scherrer K. Isolation and characterization of stable nuclear matrix preparations and associated DNA from avian erythroblasts. Biol Cell. 1988;64(1):13-22.