The multiple facets of histone H4-lysine 20 methylation

Hongbo Yang, Craig Andrew Mizzen

Research output: Contribution to journalReview article

Abstract

Antisera raised against individual sites of histone post-translational modification (PTM) have provided critical insights into the biology of many of these PTMs. However, limitations inherent to immunochemical approaches can skew results obtained with these reagents, possibly leading investigators to misjudge the role of a specific histone PTM in a given process. We have used mass spectrometry in conjunction with cell synchronization, metabolic labeling, RNA interference, and other approaches to show that the SET domain proteins PR-Set7 and Suv4-20 mediate progressive global mono-, di-, and trimethylation of lysine 20 (K20) in newly synthesized histone H4, beginning approximately at the G2/M transition, well after new H4 is deposited in replicating chromatin during S phase. Immunochemical and other approaches have implicated H4-K20 methylation in multiple processes, including gene activation, gene repression, chromatin condensation, S phase progression, mitosis, and DNA-damage checkpoint signaling. Here, we review recent data on the regulation and significance of K20 methylation.

Original languageEnglish (US)
Pages (from-to)151-161
Number of pages11
JournalBiochemistry and Cell Biology
Volume87
Issue number1
DOIs
StatePublished - Feb 1 2009

Fingerprint

Methylation
Histones
Lysine
Post Translational Protein Processing
S Phase
Chromatin
Genes
Pulse time modulation
RNA Interference
Mitosis
Labeling
Transcriptional Activation
DNA Damage
Mass spectrometry
Immune Sera
Condensation
Mass Spectrometry
Synchronization
Chemical activation
Research Personnel

Keywords

  • Chromatin
  • Epigenetics
  • Histone
  • Mass spectrometry
  • Posttranslational modification

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The multiple facets of histone H4-lysine 20 methylation. / Yang, Hongbo; Mizzen, Craig Andrew.

In: Biochemistry and Cell Biology, Vol. 87, No. 1, 01.02.2009, p. 151-161.

Research output: Contribution to journalReview article

Yang, Hongbo ; Mizzen, Craig Andrew. / The multiple facets of histone H4-lysine 20 methylation. In: Biochemistry and Cell Biology. 2009 ; Vol. 87, No. 1. pp. 151-161.
@article{4f3ddcc7d92b4801be7fd21883e18c8f,
title = "The multiple facets of histone H4-lysine 20 methylation",
abstract = "Antisera raised against individual sites of histone post-translational modification (PTM) have provided critical insights into the biology of many of these PTMs. However, limitations inherent to immunochemical approaches can skew results obtained with these reagents, possibly leading investigators to misjudge the role of a specific histone PTM in a given process. We have used mass spectrometry in conjunction with cell synchronization, metabolic labeling, RNA interference, and other approaches to show that the SET domain proteins PR-Set7 and Suv4-20 mediate progressive global mono-, di-, and trimethylation of lysine 20 (K20) in newly synthesized histone H4, beginning approximately at the G2/M transition, well after new H4 is deposited in replicating chromatin during S phase. Immunochemical and other approaches have implicated H4-K20 methylation in multiple processes, including gene activation, gene repression, chromatin condensation, S phase progression, mitosis, and DNA-damage checkpoint signaling. Here, we review recent data on the regulation and significance of K20 methylation.",
keywords = "Chromatin, Epigenetics, Histone, Mass spectrometry, Posttranslational modification",
author = "Hongbo Yang and Mizzen, {Craig Andrew}",
year = "2009",
month = "2",
day = "1",
doi = "10.1139/O08-131",
language = "English (US)",
volume = "87",
pages = "151--161",
journal = "Biochemistry and Cell Biology",
issn = "0829-8211",
publisher = "National Research Council of Canada",
number = "1",

}

TY - JOUR

T1 - The multiple facets of histone H4-lysine 20 methylation

AU - Yang, Hongbo

AU - Mizzen, Craig Andrew

PY - 2009/2/1

Y1 - 2009/2/1

N2 - Antisera raised against individual sites of histone post-translational modification (PTM) have provided critical insights into the biology of many of these PTMs. However, limitations inherent to immunochemical approaches can skew results obtained with these reagents, possibly leading investigators to misjudge the role of a specific histone PTM in a given process. We have used mass spectrometry in conjunction with cell synchronization, metabolic labeling, RNA interference, and other approaches to show that the SET domain proteins PR-Set7 and Suv4-20 mediate progressive global mono-, di-, and trimethylation of lysine 20 (K20) in newly synthesized histone H4, beginning approximately at the G2/M transition, well after new H4 is deposited in replicating chromatin during S phase. Immunochemical and other approaches have implicated H4-K20 methylation in multiple processes, including gene activation, gene repression, chromatin condensation, S phase progression, mitosis, and DNA-damage checkpoint signaling. Here, we review recent data on the regulation and significance of K20 methylation.

AB - Antisera raised against individual sites of histone post-translational modification (PTM) have provided critical insights into the biology of many of these PTMs. However, limitations inherent to immunochemical approaches can skew results obtained with these reagents, possibly leading investigators to misjudge the role of a specific histone PTM in a given process. We have used mass spectrometry in conjunction with cell synchronization, metabolic labeling, RNA interference, and other approaches to show that the SET domain proteins PR-Set7 and Suv4-20 mediate progressive global mono-, di-, and trimethylation of lysine 20 (K20) in newly synthesized histone H4, beginning approximately at the G2/M transition, well after new H4 is deposited in replicating chromatin during S phase. Immunochemical and other approaches have implicated H4-K20 methylation in multiple processes, including gene activation, gene repression, chromatin condensation, S phase progression, mitosis, and DNA-damage checkpoint signaling. Here, we review recent data on the regulation and significance of K20 methylation.

KW - Chromatin

KW - Epigenetics

KW - Histone

KW - Mass spectrometry

KW - Posttranslational modification

UR - http://www.scopus.com/inward/record.url?scp=65249157999&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=65249157999&partnerID=8YFLogxK

U2 - 10.1139/O08-131

DO - 10.1139/O08-131

M3 - Review article

C2 - 19234531

AN - SCOPUS:65249157999

VL - 87

SP - 151

EP - 161

JO - Biochemistry and Cell Biology

JF - Biochemistry and Cell Biology

SN - 0829-8211

IS - 1

ER -