Abstract
The actin-depolymerizing factor/cofilin (ADF/CFL) gene family encodes a diverse group of relatively small proteins. Once known strictly as modulators of actin filament dynamics, recent research has demonstrated that these proteins are involved in a variety of cellular processes, from signal transduction to the cytonuclear trafficking of actin. In both plant and animal lineages, expression patterns of paralogs in the ADF/CFL gene family vary among tissue types and developmental stages. In this study we use computational approaches to investigate the evolutionary forces responsible for the diversification of the ADF/CFL gene family. Estimating the rate of non-synonymous to synonymous mutations (dN/dS) across phylogenetic lineages revealed that the majority of ADF/CFL codon positions were under strong purifying selection, with rare episodic events of accelerated protein evolution. In both plants and animals these instances of accelerated evolution were ADF/CFL subclass specific, and all of the sites under selection were located in regions of the protein that could serve in new functional roles. We suggest these sites may have been important in the functional diversification of ADF/CFL proteins.
Highlights
The actin cytoskeleton is one of the most dynamic features in a eukaryotic cell
A variety of classes of actin binding proteins are found in plants and animals that facilitate the dynamic nature of actin, one of which is encoded by the actin-depolymerizing factor/cofilin (ADF/CFL) gene family
ADF/ CFLs comprise a group of relatively small proteins approximately 13–19 kDa in size [1] with a shared conserved structural motif known as the actin-depolymerizing factor homology (ADF-H) domain [2, 3] that is characterized by the presence of five β-strands that lie internal to four or more α-helices [3]
Summary
The actin cytoskeleton is one of the most dynamic features in a eukaryotic cell. It is involved in a number of important and diverse cellular processes such as organelle movement, exo- and endocytosis, nuclear trafficking, and chromatin remodeling. A variety of classes of actin binding proteins are found in plants and animals that facilitate the dynamic nature of actin, one of which is encoded by the actin-depolymerizing factor/cofilin (ADF/CFL) gene family. ADF/CFLs were first described as proteins that bind and sever actin monomers from F-actin filaments, but this ADP-actin filament severing activity is only present at low cellular concentrations of ADF/CFL [1, 4, 5]. At intermediate concentrations ADF/CFLs have been shown to stabilize filaments, and at high concentrations they
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