Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center

Sue Ying Huang; William T. Garrard

doi:10.1016/0014-5793(86)81229-7

Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center

Sue Ying Huang, William T. Garrard

Molecular Biology

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Digestion of nuclei at 4°C with micrococcal nuclease results in significant intranucleosomal cleavage compared to digestion conducted at 37°C. Employing nucleoprotein gel electrophoresis in one dimension followed by DNA electrophoresis in a second dimension, we demonstrate that such temperature-sensitive, internal cleavage predominantly occurs about 20 bp from the nucleosome center. We suggest that lower temperatures reduce the stability of hydrophobic interactions within the histone octamer and lead to a conformational alteration in nucleosomes that is detected by micrococcal nuclease.

Original language	English (US)
Pages (from-to)	89-91
Number of pages	3
Journal	FEBS Letters
Volume	199
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(86)81229-7
State	Published - Apr 7 1986

Keywords

Chromatin structure
Half-nucleosome
Histone octamer
Micrococcal nuclease
Nucleosome
Two-dimensional electrophoresis

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(86)81229-7

Cite this

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title = "Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center",

abstract = "Digestion of nuclei at 4°C with micrococcal nuclease results in significant intranucleosomal cleavage compared to digestion conducted at 37°C. Employing nucleoprotein gel electrophoresis in one dimension followed by DNA electrophoresis in a second dimension, we demonstrate that such temperature-sensitive, internal cleavage predominantly occurs about 20 bp from the nucleosome center. We suggest that lower temperatures reduce the stability of hydrophobic interactions within the histone octamer and lead to a conformational alteration in nucleosomes that is detected by micrococcal nuclease.",

keywords = "Chromatin structure, Half-nucleosome, Histone octamer, Micrococcal nuclease, Nucleosome, Two-dimensional electrophoresis",

author = "Huang, {Sue Ying} and Garrard, {William T.}",

note = "Funding Information: We are gratefult o V.C. Blasquezf or reviewa nd to M. Rotondi for preparationo f this manuscript. This work was supported by grants GM22201, GM29935,G M25829a nd GM31689f rom NIH and grant I-823 from The Robert A. Welch Foundation.",

year = "1986",

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doi = "10.1016/0014-5793(86)81229-7",

language = "English (US)",

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T1 - Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center

AU - Huang, Sue Ying

AU - Garrard, William T.

N1 - Funding Information: We are gratefult o V.C. Blasquezf or reviewa nd to M. Rotondi for preparationo f this manuscript. This work was supported by grants GM22201, GM29935,G M25829a nd GM31689f rom NIH and grant I-823 from The Robert A. Welch Foundation.

PY - 1986/4/7

Y1 - 1986/4/7

N2 - Digestion of nuclei at 4°C with micrococcal nuclease results in significant intranucleosomal cleavage compared to digestion conducted at 37°C. Employing nucleoprotein gel electrophoresis in one dimension followed by DNA electrophoresis in a second dimension, we demonstrate that such temperature-sensitive, internal cleavage predominantly occurs about 20 bp from the nucleosome center. We suggest that lower temperatures reduce the stability of hydrophobic interactions within the histone octamer and lead to a conformational alteration in nucleosomes that is detected by micrococcal nuclease.

AB - Digestion of nuclei at 4°C with micrococcal nuclease results in significant intranucleosomal cleavage compared to digestion conducted at 37°C. Employing nucleoprotein gel electrophoresis in one dimension followed by DNA electrophoresis in a second dimension, we demonstrate that such temperature-sensitive, internal cleavage predominantly occurs about 20 bp from the nucleosome center. We suggest that lower temperatures reduce the stability of hydrophobic interactions within the histone octamer and lead to a conformational alteration in nucleosomes that is detected by micrococcal nuclease.

KW - Chromatin structure

KW - Half-nucleosome

KW - Histone octamer

KW - Micrococcal nuclease

KW - Nucleosome

KW - Two-dimensional electrophoresis

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Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center

Abstract

Keywords

ASJC Scopus subject areas

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