Skip Navigation


MBE Advance Access originally published online on August 16, 2007
Molecular Biology and Evolution 2007 24(10):2254-2265; doi:10.1093/molbev/msm168
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
24/10/2254    most recent
msm168v1
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 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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Virel, A.
Right arrow Articles by Backman, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Virel, A.
Right arrow Articles by Backman, L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2007. 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 Articles

A Comparative and Phylogenetic Analysis of the {alpha}-Actinin Rod Domain

Ana Virel and Lars Backman

Department of Biochemistry, Umeå University, Umeå, Sweden

E-mail: lars.backman{at}chem.umu.se.

Accepted for publication July 16, 2007.

{alpha}-Actinin is a ubiquitous actin-binding protein, composed of 3 domains; an actin-binding domain and a calcium-binding domain at the termini, connected by a rod domain composed by 1, 2, or 4 spectrin repeats (SRs). To understand how the rod domain has evolved during evolution, we have analyzed and compared the amino acid residue heterogeneity and phylogeny of the SRs of {alpha}-actinins of vertebrates, invertebrates, fungi, and several protozoa.

The repeats of vertebrate {alpha}-actinins show a high degree of similarity, whereas repeats of invertebrates, fungi, and, in particular, of protozoa are more divergent.

In the phylogeny, SR1 of all species were clustered together, independent of the number of repeats in the protein. It was also obvious that the second and last repeat in fungi (SR2) grouped with the fourth and last repeat of vertebrates and invertebrates (SR4).

Therefore, the phylogeny implied that the rod domain of the cenancestral {alpha}-actinin only contained one SR. It was also obvious that SR2 of fungi are related to SR4 of vertebrates and invertebrates, implying that in the second intragenic duplication 2 repeats (i.e., what become SR2 and SR3) were inserted between the initial 2 repeats that become SR1 and SR4.

Key Words: {alpha}-actinin • phylogeny • evolution • spectrin superfamily • spectrin repeat

Michele Vendruscolo, Associate Editor


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
A. J. Baines, P. A. Bignone, M. D.A. King, A. M. Maggs, P. M. Bennett, J. C. Pinder, and G. W. Phillips
The CKK Domain (DUF1781) Binds Microtubules and Defines the CAMSAP/ssp4 Family of Animal Proteins
Mol. Biol. Evol., September 1, 2009; 26(9): 2005 - 2014.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
J. Wang, H. Hu, S. Wang, J. Shi, S. Chen, H. Wei, X. Xu, and L. Lu
The important role of actinin-like protein (AcnA) in cytokinesis and apical dominance of hyphal cells in Aspergillus nidulans
Microbiology, August 1, 2009; 155(8): 2714 - 2725.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
D. Wilson, R. Pethica, Y. Zhou, C. Talbot, C. Vogel, M. Madera, C. Chothia, and J. Gough
SUPERFAMILY--sophisticated comparative genomics, data mining, visualization and phylogeny
Nucleic Acids Res., January 1, 2009; 37(suppl_1): D380 - D386.
[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.