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A Comparative and Phylogenetic Analysis of the {alpha}-Actinin Rod Domain
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
2007 (English)In: Molecular Biology and Evolution, Vol. 24, no 10, 2254-65 p.Article in journal (Refereed) Published
Abstract [en]

-actinin is a ubiquitous actin-binding protein, composed of three domains; an actin-binding domain and a calcium-binding domain at the termini, connected by a rod domain composed by one, two or four spectrin repeats (SR). To understand how the rod domain has evolved during evolution we have analysed and compared the amino acid residue heterogeneity and phylogeny of the spectrin repeats of -actinins of vertebrates, invertebrates, fungus and several protozoa.

The repeats of vertebrate -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 -actinin only contained one spectrin repeat. It was also obvious that SR2 of fungi are related to SR4 of vertebrates and invertebrates, implying that in the second intragenic duplication two repeats (i.e. what become SR2 and SR3) were inserted between the initial two repeats that become SR1 and SR4.

Place, publisher, year, edition, pages
2007. Vol. 24, no 10, 2254-65 p.
Keyword [en]
-actinin, phylogeny, evolution, spectrin super-family, spectrin repeat
Identifiers
URN: urn:nbn:se:umu:diva-16154DOI: doi:10.1093/molbev/msm168OAI: oai:DiVA.org:umu-16154DiVA: diva2:155827
Note
MBE Advance Access published online on August 16, 2007Available from: 2007-10-11 Created: 2007-10-11 Last updated: 2011-01-11Bibliographically approved

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CiteExportLink to record
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