English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Probing the acetylation code of histone H4.

Lang, D., Schümann, M., Gelato, K., Fischle, W., Schwarzer, D., & Krause, E. (2013). Probing the acetylation code of histone H4. Proteomics, 13(20), 2989-2997. doi:10.1002/pmic.201200568.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-7AA1-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CB6D-B
Genre: Journal Article

Files

show Files
hide Files
:
1850500.pdf (Publisher version), 507KB
 
File Permalink:
-
Name:
1850500.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-1.xlsx (Supplementary material), 434KB
Name:
1850500-Suppl-1.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-2.xlsx (Supplementary material), 367KB
Name:
1850500-Suppl-2.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-3.xlsx (Supplementary material), 431KB
Name:
1850500-Suppl-3.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-4.xlsx (Supplementary material), 406KB
Name:
1850500-Suppl-4.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-5.xlsx (Supplementary material), 459KB
Name:
1850500-Suppl-5.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-6.xlsx (Supplementary material), 526KB
Name:
1850500-Suppl-6.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-7.xlsx (Supplementary material), 232KB
Name:
1850500-Suppl-7.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1850500-Suppl-8.xlsx (Supplementary material), 277KB
Name:
1850500-Suppl-8.xlsx
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.openxmlformats-officedocument.spreadsheetml.sheet / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Lang, D., Author
Schümann, M., Author
Gelato, K.1, Author              
Fischle, W.1, Author              
Schwarzer, D., Author
Krause, E., Author
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

Content

show
hide
Free keywords: Cell biology / Chromatin / Histone acetylation / Interactome analysis / Quantitative mass spectrometry / SILAC
 Abstract: Histone modifications play crucial roles in genome regulation with lysine acetylation being implicated in transcriptional control. Here we report a proteome-wide investigation of the acetylation-dependent protein–protein interactions of the N-terminal tail of histone H4. Quantitative peptide-based affinity MS experiments using the SILAC approach determined the interactomes of H4 tails monoacetylated at the four known acetylation sites K5, K8, K12, and K16, bis-acetylated at K5/K12, triple-acetylated at K8/12/16 and fully tetra-acetylated. A set of 29 proteins was found enriched on the fully acetylated H4 tail while specific binders of the mono and bis-acetylated tails were barely detectable. These observations are in good agreement with earlier reports indicating that the H4 acetylation state establishes its regulatory effects in a cumulative manner rather than via site-specific recruitment of regulatory proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2013-10-082013-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pmic.201200568
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proteomics
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 13 (20) Sequence Number: - Start / End Page: 2989 - 2997 Identifier: -