English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Analysis of phosphorylation-dependent protein-protein interactions of histone H3.

Klingberg, R., Jost, J. O., Schümann, M., Gelato, K. A., Fischle, W., Krause, E., et al. (2015). Analysis of phosphorylation-dependent protein-protein interactions of histone H3. ACS Chemical Biology, 10(1), 138-145. doi:10.1021/cb500563n.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-6C23-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-F619-1
Genre: Journal Article

Files

show Files
hide Files
:
2111455.pdf (Publisher version), 3MB
 
File Permalink:
-
Name:
2111455.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:
-
:
2111455_Suppl_1.pdf (Supplementary material), 355KB
Name:
2111455_Suppl_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2111455_Suppl_2.xls (Supplementary material), 5MB
Name:
2111455_Suppl_2.xls
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.ms-excel / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2111455_Suppl_3.xls (Supplementary material), 4MB
Name:
2111455_Suppl_3.xls
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/vnd.ms-excel / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://pubs.acs.org/doi/pdf/10.1021/cb500563n (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Klingberg, R., Author
Jost, J. O., Author
Schümann, M., Author
Gelato, K. A.1, Author              
Fischle, W.1, Author              
Krause, E., Author
Schwarzer, D.2, Author              
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              
2Research Group of Reaction Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578601              

Content

show
hide
Free keywords: -
 Abstract: Multiple posttranslational modifications (PTMs) of histone proteins including site-specific phosphorylation of serine and threonine residues govern the accessibility of chromatin. According to the histone code theory, PTMs recruit regulatory proteins or block their access to chromatin. Here, we report a general strategy for simultaneous analysis of both of these effects based on a SILAC MS scheme. We applied this approach for studying the biochemical role of phosphorylated S10 of histone H3. Differential pull-down experiments with H3-tails synthesized from l- and d-amino acids uncovered that histone acetyltransferase 1 (HAT1) and retinoblastoma-binding protein 7 (RBBP7) are part of the protein network, which interacts with the unmodified H3-tail. An additional H3-derived bait containing the nonhydrolyzable phospho-serine mimic phosphonomethylen-alanine (Pma) at S10 recruited several isoforms of the 14-3-3 family and blocked the recruitment of HAT1 and RBBP7 to the unmodified H3-tail. Our observations provide new insights into the many functions of H3S10 phosphorylation. In addition, the outlined methodology is generally applicable for studying specific binding partners of unmodified histone tails.

Details

show
hide
Language(s): eng - English
 Dates: 2014-10-202015-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/cb500563n
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: ACS Chemical Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 10 (1) Sequence Number: - Start / End Page: 138 - 145 Identifier: -