Interaction of MAR‐sequences with nuclear matrix proteins

Maria Ivanchenko, Zoya V Avramova

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The recent discovery of DNA sequences responsible for the specific attachment of chromosomal DNA to the nuclear skeleton (MARs/SARs) was an important step towards our understanding of the functional and structural organization of eukaryotic chromatin [Mirkovitch et al.: Cell 44:273–282, 1984; Cockerill and Garrard: Cell 44:273–282, 1986]. A most important question, however, remains the nature of the matrix proteins involved in the specific binding of the MARs. It has been shown that topoisomerase II and histone H1 were capable of a specific interaction with SARs by the formation of precipitable complexes [Adachi et al.; EMBO J 8:3997–4006, 1989; lzaurralde et al.: J Mol Biol 210:573–585, 1989]. Here, applying a different approach, we were able to “visualize” some of the skeletal proteins recognizing and specifically binding MAR‐sequences. It is shown that the major matrix proteins are practically the same in both salt‐ and LIS‐extracted matrices. However, the relative MAR‐binding activity of the individual protein components may be different, depending on the method of matrix preparation. The immunological approach applied here allowed us to identify some of the individual MAR‐binding matrix proteins. Histone H1 and nuclear actin are shown to be not only important components of the matrix, but to be involved in a highly efficient interaction with MAR‐sequences as well. Evidence is presented that proteins recognized by the anti‐HMG antibodies also participate in Mar‐interactions. © 1992 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)190-200
Number of pages11
JournalJournal of Cellular Biochemistry
Volume50
Issue number2
DOIs
StatePublished - Jan 1 1992

Fingerprint

Nuclear Matrix-Associated Proteins
Proteins
Histones
Type II DNA Topoisomerase
DNA sequences
Skeleton
Chromatin
Actins
Salts
Antibodies
DNA

Keywords

  • HMG proteins
  • MAR sequences
  • histone H1
  • matrix proteins
  • nuclear actin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Interaction of MAR‐sequences with nuclear matrix proteins. / Ivanchenko, Maria; Avramova, Zoya V.

In: Journal of Cellular Biochemistry, Vol. 50, No. 2, 01.01.1992, p. 190-200.

Research output: Contribution to journalArticle

@article{71c23c6d0265470a8b7da4ef11fb06f7,
title = "Interaction of MAR‐sequences with nuclear matrix proteins",
abstract = "The recent discovery of DNA sequences responsible for the specific attachment of chromosomal DNA to the nuclear skeleton (MARs/SARs) was an important step towards our understanding of the functional and structural organization of eukaryotic chromatin [Mirkovitch et al.: Cell 44:273–282, 1984; Cockerill and Garrard: Cell 44:273–282, 1986]. A most important question, however, remains the nature of the matrix proteins involved in the specific binding of the MARs. It has been shown that topoisomerase II and histone H1 were capable of a specific interaction with SARs by the formation of precipitable complexes [Adachi et al.; EMBO J 8:3997–4006, 1989; lzaurralde et al.: J Mol Biol 210:573–585, 1989]. Here, applying a different approach, we were able to “visualize” some of the skeletal proteins recognizing and specifically binding MAR‐sequences. It is shown that the major matrix proteins are practically the same in both salt‐ and LIS‐extracted matrices. However, the relative MAR‐binding activity of the individual protein components may be different, depending on the method of matrix preparation. The immunological approach applied here allowed us to identify some of the individual MAR‐binding matrix proteins. Histone H1 and nuclear actin are shown to be not only important components of the matrix, but to be involved in a highly efficient interaction with MAR‐sequences as well. Evidence is presented that proteins recognized by the anti‐HMG antibodies also participate in Mar‐interactions. {\circledC} 1992 Wiley‐Liss, Inc.",
keywords = "HMG proteins, MAR sequences, histone H1, matrix proteins, nuclear actin",
author = "Maria Ivanchenko and Avramova, {Zoya V}",
year = "1992",
month = "1",
day = "1",
doi = "10.1002/jcb.240500209",
language = "English (US)",
volume = "50",
pages = "190--200",
journal = "Journal of Cellular Biochemistry",
issn = "0730-2312",
publisher = "Wiley-Liss Inc.",
number = "2",

}

TY - JOUR

T1 - Interaction of MAR‐sequences with nuclear matrix proteins

AU - Ivanchenko, Maria

AU - Avramova, Zoya V

PY - 1992/1/1

Y1 - 1992/1/1

N2 - The recent discovery of DNA sequences responsible for the specific attachment of chromosomal DNA to the nuclear skeleton (MARs/SARs) was an important step towards our understanding of the functional and structural organization of eukaryotic chromatin [Mirkovitch et al.: Cell 44:273–282, 1984; Cockerill and Garrard: Cell 44:273–282, 1986]. A most important question, however, remains the nature of the matrix proteins involved in the specific binding of the MARs. It has been shown that topoisomerase II and histone H1 were capable of a specific interaction with SARs by the formation of precipitable complexes [Adachi et al.; EMBO J 8:3997–4006, 1989; lzaurralde et al.: J Mol Biol 210:573–585, 1989]. Here, applying a different approach, we were able to “visualize” some of the skeletal proteins recognizing and specifically binding MAR‐sequences. It is shown that the major matrix proteins are practically the same in both salt‐ and LIS‐extracted matrices. However, the relative MAR‐binding activity of the individual protein components may be different, depending on the method of matrix preparation. The immunological approach applied here allowed us to identify some of the individual MAR‐binding matrix proteins. Histone H1 and nuclear actin are shown to be not only important components of the matrix, but to be involved in a highly efficient interaction with MAR‐sequences as well. Evidence is presented that proteins recognized by the anti‐HMG antibodies also participate in Mar‐interactions. © 1992 Wiley‐Liss, Inc.

AB - The recent discovery of DNA sequences responsible for the specific attachment of chromosomal DNA to the nuclear skeleton (MARs/SARs) was an important step towards our understanding of the functional and structural organization of eukaryotic chromatin [Mirkovitch et al.: Cell 44:273–282, 1984; Cockerill and Garrard: Cell 44:273–282, 1986]. A most important question, however, remains the nature of the matrix proteins involved in the specific binding of the MARs. It has been shown that topoisomerase II and histone H1 were capable of a specific interaction with SARs by the formation of precipitable complexes [Adachi et al.; EMBO J 8:3997–4006, 1989; lzaurralde et al.: J Mol Biol 210:573–585, 1989]. Here, applying a different approach, we were able to “visualize” some of the skeletal proteins recognizing and specifically binding MAR‐sequences. It is shown that the major matrix proteins are practically the same in both salt‐ and LIS‐extracted matrices. However, the relative MAR‐binding activity of the individual protein components may be different, depending on the method of matrix preparation. The immunological approach applied here allowed us to identify some of the individual MAR‐binding matrix proteins. Histone H1 and nuclear actin are shown to be not only important components of the matrix, but to be involved in a highly efficient interaction with MAR‐sequences as well. Evidence is presented that proteins recognized by the anti‐HMG antibodies also participate in Mar‐interactions. © 1992 Wiley‐Liss, Inc.

KW - HMG proteins

KW - MAR sequences

KW - histone H1

KW - matrix proteins

KW - nuclear actin

UR - http://www.scopus.com/inward/record.url?scp=0026758231&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026758231&partnerID=8YFLogxK

U2 - 10.1002/jcb.240500209

DO - 10.1002/jcb.240500209

M3 - Article

VL - 50

SP - 190

EP - 200

JO - Journal of Cellular Biochemistry

JF - Journal of Cellular Biochemistry

SN - 0730-2312

IS - 2

ER -