MBE Advance Access published online on March 10, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh094
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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1 Biochemistry, Umeå University, SE-901 87 Umeå, Sweden
* To whom correspondence should be addressed. E-mail: lars.backman{at}chem.umu.se.
The N-terminal actin-binding domain of We have found some atypical Further, the evolutionary gene tree of Since Key Words:
© 2004 Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved.
Original Articles
Molecular Evolution and Structure of
-Actinin
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Abstract
-actinin is connected to the C-terminal EF-hands by a rod domain. Due to its ability to form dimers,
-actinin can cross-link actin filaments in muscle cells as well as in non-muscle cells. In the prototypic
-actinins the rod domain contains four triple helical bundles, or so called spectrin repeats.
-actinins in early diverging organisms, such as protozoa and yeast, where the rod domain contains one or two spectrin repeats, respectively. This implies that the four repeats present in modern
-actinins arose after two consecutive intragenic duplications from a
-actinin with a single repeat.
-actinins show that the appearance of four distinct
-actinin isoforms may have occurred after the vertebrate invertebrate split. The topology of the tree lends support to the hypothesis that two rounds (2R) of genome duplication occurred early in the vertebrate radiation. The phylogeny also considers these atypical isoforms as the most basal to
-actinins of vertebrates and other eukaryotes. The analysis also positioned
-actinin of the fungi Encephalitozoo cuniculi close to the protozoa, supporting the suggestion that microsporidia are early eukaryotes.
-actinin is considered as the basal member of the spectrin family our studies will improve the understanding of the origin and evolution of this super-family.
-actinin, phylogeny, evolution, spectrin super-family, spectrin repeat
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