Skip Navigation


MBE Advance Access originally published online on January 23, 2006
Molecular Biology and Evolution 2006 23(4):734-743; doi:10.1093/molbev/msj091
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
23/4/734    most recent
msj091v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Weiner, J.
Right arrow Articles by Bornberg-Bauer, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weiner, J., 3rd
Right arrow Articles by Bornberg-Bauer, E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Article

Evolution of Circular Permutations in Multidomain Proteins

January Weiner, 3rd and Erich Bornberg-Bauer

Division of Bioinformatics, School of Biological Sciences, University of Münster, Schlossplatz 4, Münster, Germany

E-mail: january{at}uni-muenster.de.

Modular rearrangements play an important role in protein evolution. Functional modules, often tantamount to structural domains or smaller fragments, are in many cases well conserved but reoccur in a different order and across many protein families. The underlying genetic mechanisms are gene duplication, fusion, and loss of sequence fragments. As a consequence, the sequential order of domains can be inverted, leading to what is known as circularly permutated proteins. Using a recently developed algorithm, we have identified a large number of such rearrangements and analyzed their evolutionary history. We searched for examples which have arisen by one of the three postulated mechanisms: independent fusion/fission, "duplication/deletion," and plasmid-mediated "cut and paste." We conclude that all three mechanisms can be observed, with the independent fusion/fission being the most frequent. This can be partly attributed to highly mobile domains. Duplication/deletion has been found in modular proteins such as peptide synthases.

Key Words: circular permutation • domains • modular evolution • rearrangement


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol Biol EvolHome page
K. Forslund, A. Henricson, V. Hollich, and E. L. L. Sonnhammer
Domain Tree-Based Analysis of Protein Architecture Evolution
Mol. Biol. Evol., February 1, 2008; 25(2): 254 - 264.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
S. Pasek, J.-L. Risler, and P. Brezellec
Gene fusion/fission is a major contributor to evolution of multi-domain bacterial proteins
Bioinformatics, June 15, 2006; 22(12): 1418 - 1423.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.