English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  On the origin of the histone fold.

Alva, V., Ammelburg, M., Söding, J., & Lupas, A. N. (2007). On the origin of the histone fold. BMC Structural Biology, 7: 17. doi:10.1186/1472-6807-7-17.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0017-E701-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C599-A
Genre: Journal Article

Files

show Files
hide Files
:
1944240.pdf (Publisher version), 3MB
Name:
1944240.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Alva, V.1, Author
Ammelburg, M.1, Author
Söding, J.2, Author              
Lupas, A. N.1, Author
Affiliations:
1external, ou_persistent22              
2Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              

Content

show
hide
Free keywords: -
 Abstract: Background Histones organize the genomic DNA of eukaryotes into chromatin. The four core histone subunits consist of two consecutive helix-strand-helix motifs and are interleaved into heterodimers with a unique fold. We have searched for the evolutionary origin of this fold using sequence and structure comparisons, based on the hypothesis that folded proteins evolved by combination of an ancestral set of peptides, the antecedent domain segments. Results Our results suggest that an antecedent domain segment, corresponding to one helix-strand-helix motif, gave rise divergently to the N-terminal substrate recognition domain of Clp/Hsp100 proteins and to the helical part of the extended ATPase domain found in AAA+ proteins. The histone fold arose subsequently from the latter through a 3D domain-swapping event. To our knowledge, this is the first example of a genetically fixed 3D domain swap that led to the emergence of a protein family with novel properties, establishing domain swapping as a mechanism for protein evolution. Conclusion The helix-strand-helix motif common to these three folds provides support for our theory of an 'ancient peptide world' by demonstrating how an ancestral fragment can give rise to 3 different folds.

Details

show
hide
Language(s): eng - English
 Dates: 2007-03-28
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1186/1472-6807-7-17
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: BMC Structural Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : BioMed Central
Pages: - Volume / Issue: 7 Sequence Number: 17 Start / End Page: - Identifier: ISSN: 1471-2237
CoNE: /journals/resource/1000000000223970_2