Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome

Jongseong Kim, Jaehyoun Lee, Tae-hee Lee

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit.

Original languageEnglish (US)
Pages (from-to)15001-15005
Number of pages5
JournalJournal of Physical Chemistry B
Volume119
Issue number48
DOIs
StatePublished - Dec 3 2015

Fingerprint

acetylation
Acetylation
Nucleosomes
lysine
Lysine
DNA
deoxyribonucleic acid
Histones
dynamic structural analysis
Structural dynamics
proteins
Proteins
Chemical modification

All Science Journal Classification (ASJC) codes

  • Surfaces, Coatings and Films
  • Physical and Theoretical Chemistry
  • Materials Chemistry

Cite this

Kim, Jongseong ; Lee, Jaehyoun ; Lee, Tae-hee. / Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome. In: Journal of Physical Chemistry B. 2015 ; Vol. 119, No. 48. pp. 15001-15005.
@article{b8be427b521a4f08b89fbdf292e30657,
title = "Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome",
abstract = "The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit.",
author = "Jongseong Kim and Jaehyoun Lee and Tae-hee Lee",
year = "2015",
month = "12",
day = "3",
doi = "10.1021/acs.jpcb.5b09734",
language = "English (US)",
volume = "119",
pages = "15001--15005",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "48",

}

Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome. / Kim, Jongseong; Lee, Jaehyoun; Lee, Tae-hee.

In: Journal of Physical Chemistry B, Vol. 119, No. 48, 03.12.2015, p. 15001-15005.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome

AU - Kim, Jongseong

AU - Lee, Jaehyoun

AU - Lee, Tae-hee

PY - 2015/12/3

Y1 - 2015/12/3

N2 - The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit.

AB - The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit.

UR - http://www.scopus.com/inward/record.url?scp=84948845997&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84948845997&partnerID=8YFLogxK

U2 - 10.1021/acs.jpcb.5b09734

DO - 10.1021/acs.jpcb.5b09734

M3 - Article

C2 - 26575591

AN - SCOPUS:84948845997

VL - 119

SP - 15001

EP - 15005

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 48

ER -