Chromatin structure in granulocytes. A link between tight compaction and accumulation of a heterochromatin-associated protein (MENT)

Sergei A. Grigoryev, Christopher L. Woodcock

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

To study the mechanism of heterochromatin formation in vertebrate cells, we isolated nuclei from chicken polymorphonuclear granulocytes and examined the chromatin organization. We found granulocyte chromatin to remain insoluble after nuclease digestion and to be resistant to swelling in low salt/high pH media. Both insolubility and resistance to swelling were lost after washing with 0.3 M NaCl, a procedure that released two abundant tissue- specific proteins from granulocyte nuclei. One of them (42 kDa) is identified as MENT, a protein previously shown to be associated with repressed chromatin from mature chicken erythrocytes. We show that MENT is immunolocalized in granulocyte heterochromatin, where it is one of the most abundant chromatin proteins (~2 molecules/200 base pairs of DNA). MENT is the first nuclear protein structurally related to the serine protease inhibitor family. The other abundant protein is similar to or identical with mim-1, a myeloid- specific protein that is known to be stored in cell granules and to associate with isolated nuclei. MENT (but not mim-1) binds chromatin and free DNA, and, at its physiological protein/DNA ratio, enhances compaction and the reversible Mg2+-dependent self-association of nucleosome arrays. MENT appears to promote the formation of heterochromatin by acting as a 'glue' within and between chains of nucleosomes.

Original languageEnglish (US)
Pages (from-to)3082-3089
Number of pages8
JournalJournal of Biological Chemistry
Volume273
Issue number5
DOIs
StatePublished - Jan 30 1998

Fingerprint

Heterochromatin
Granulocytes
Chromatin
Compaction
Proteins
Nucleosomes
Swelling
Chickens
DNA
Serine Proteinase Inhibitors
Glues
Nuclear Proteins
Cell Nucleus
Washing
Base Pairing
Adhesives
Vertebrates
Digestion
Solubility
Salts

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{f63eb2453f4f4389b1622a851038fcc7,
title = "Chromatin structure in granulocytes. A link between tight compaction and accumulation of a heterochromatin-associated protein (MENT)",
abstract = "To study the mechanism of heterochromatin formation in vertebrate cells, we isolated nuclei from chicken polymorphonuclear granulocytes and examined the chromatin organization. We found granulocyte chromatin to remain insoluble after nuclease digestion and to be resistant to swelling in low salt/high pH media. Both insolubility and resistance to swelling were lost after washing with 0.3 M NaCl, a procedure that released two abundant tissue- specific proteins from granulocyte nuclei. One of them (42 kDa) is identified as MENT, a protein previously shown to be associated with repressed chromatin from mature chicken erythrocytes. We show that MENT is immunolocalized in granulocyte heterochromatin, where it is one of the most abundant chromatin proteins (~2 molecules/200 base pairs of DNA). MENT is the first nuclear protein structurally related to the serine protease inhibitor family. The other abundant protein is similar to or identical with mim-1, a myeloid- specific protein that is known to be stored in cell granules and to associate with isolated nuclei. MENT (but not mim-1) binds chromatin and free DNA, and, at its physiological protein/DNA ratio, enhances compaction and the reversible Mg2+-dependent self-association of nucleosome arrays. MENT appears to promote the formation of heterochromatin by acting as a 'glue' within and between chains of nucleosomes.",
author = "Grigoryev, {Sergei A.} and Woodcock, {Christopher L.}",
year = "1998",
month = "1",
day = "30",
doi = "10.1074/jbc.273.5.3082",
language = "English (US)",
volume = "273",
pages = "3082--3089",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

Chromatin structure in granulocytes. A link between tight compaction and accumulation of a heterochromatin-associated protein (MENT). / Grigoryev, Sergei A.; Woodcock, Christopher L.

In: Journal of Biological Chemistry, Vol. 273, No. 5, 30.01.1998, p. 3082-3089.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Chromatin structure in granulocytes. A link between tight compaction and accumulation of a heterochromatin-associated protein (MENT)

AU - Grigoryev, Sergei A.

AU - Woodcock, Christopher L.

PY - 1998/1/30

Y1 - 1998/1/30

N2 - To study the mechanism of heterochromatin formation in vertebrate cells, we isolated nuclei from chicken polymorphonuclear granulocytes and examined the chromatin organization. We found granulocyte chromatin to remain insoluble after nuclease digestion and to be resistant to swelling in low salt/high pH media. Both insolubility and resistance to swelling were lost after washing with 0.3 M NaCl, a procedure that released two abundant tissue- specific proteins from granulocyte nuclei. One of them (42 kDa) is identified as MENT, a protein previously shown to be associated with repressed chromatin from mature chicken erythrocytes. We show that MENT is immunolocalized in granulocyte heterochromatin, where it is one of the most abundant chromatin proteins (~2 molecules/200 base pairs of DNA). MENT is the first nuclear protein structurally related to the serine protease inhibitor family. The other abundant protein is similar to or identical with mim-1, a myeloid- specific protein that is known to be stored in cell granules and to associate with isolated nuclei. MENT (but not mim-1) binds chromatin and free DNA, and, at its physiological protein/DNA ratio, enhances compaction and the reversible Mg2+-dependent self-association of nucleosome arrays. MENT appears to promote the formation of heterochromatin by acting as a 'glue' within and between chains of nucleosomes.

AB - To study the mechanism of heterochromatin formation in vertebrate cells, we isolated nuclei from chicken polymorphonuclear granulocytes and examined the chromatin organization. We found granulocyte chromatin to remain insoluble after nuclease digestion and to be resistant to swelling in low salt/high pH media. Both insolubility and resistance to swelling were lost after washing with 0.3 M NaCl, a procedure that released two abundant tissue- specific proteins from granulocyte nuclei. One of them (42 kDa) is identified as MENT, a protein previously shown to be associated with repressed chromatin from mature chicken erythrocytes. We show that MENT is immunolocalized in granulocyte heterochromatin, where it is one of the most abundant chromatin proteins (~2 molecules/200 base pairs of DNA). MENT is the first nuclear protein structurally related to the serine protease inhibitor family. The other abundant protein is similar to or identical with mim-1, a myeloid- specific protein that is known to be stored in cell granules and to associate with isolated nuclei. MENT (but not mim-1) binds chromatin and free DNA, and, at its physiological protein/DNA ratio, enhances compaction and the reversible Mg2+-dependent self-association of nucleosome arrays. MENT appears to promote the formation of heterochromatin by acting as a 'glue' within and between chains of nucleosomes.

UR - http://www.scopus.com/inward/record.url?scp=0032579273&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032579273&partnerID=8YFLogxK

U2 - 10.1074/jbc.273.5.3082

DO - 10.1074/jbc.273.5.3082

M3 - Article

C2 - 9446625

AN - SCOPUS:0032579273

VL - 273

SP - 3082

EP - 3089

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 5

ER -