Roots of angiosperm formins: The evolutionary history of plant FH2 domain-containing proteins
Open Access
- 22 April 2008
- journal article
- Published by Springer Science and Business Media LLC in BMC Evolutionary Biology
- Vol. 8 (1), 115
- https://doi.org/10.1186/1471-2148-8-115
Abstract
Shuffling of modular protein domains is an important source of evolutionary innovation. Formins are a family of actin-organizing proteins that share a conserved FH2 domain but their overall domain architecture differs dramatically between opisthokonts (metazoans and fungi) and plants. We performed a phylogenomic analysis of formins in most eukaryotic kingdoms, aiming to reconstruct an evolutionary scenario that may have produced the current diversity of domain combinations with focus on the origin of the angiosperm formin architectures. The Rho GTPase-binding domain (GBD/FH3) reported from opisthokont and Dictyostelium formins was found in all lineages except plants, suggesting its ancestral character. Instead, mosses and vascular plants possess the two formin classes known from angiosperms: membrane-anchored Class I formins and Class II formins carrying a PTEN-like domain. PTEN-related domains were found also in stramenopile formins, where they have been probably acquired independently rather than by horizontal transfer, following a burst of domain rearrangements in the chromalveolate lineage. A novel RhoGAP-related domain was identified in some algal, moss and lycophyte (but not angiosperm) formins that define a specific branch (Class III) of the formin family. We propose a scenario where formins underwent multiple domain rearrangements in several eukaryotic lineages, especially plants and chromalveolates. In plants this replaced GBD/FH3 by a probably inactive RhoGAP-like domain, preserving a formin-mediated association between (membrane-anchored) Rho GTPases and the actin cytoskeleton. Subsequent amplification of formin genes, possibly coincident with the expansion of plants to dry land, was followed by acquisition of alternative membrane attachment mechanisms present in extant Class I and Class II formins, allowing later loss of the RhoGAP-like domain-containing formins in angiosperms.Keywords
This publication has 96 references indexed in Scilit:
- Locating proteins in the cell using TargetP, SignalP and related toolsNature Protocols, 2007
- Kalign, Kalignvu and Mumsa: web servers for multiple sequence alignmentNucleic Acids Research, 2006
- The SWISS-MODEL workspace: a web-based environment for protein structure homology modellingBioinformatics, 2005
- Formin proteins: a domain-based approachTrends in Biochemical Sciences, 2005
- Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10DNature, 2004
- The Arabidopsis Information Resource (TAIR): a model organism database providing a centralized, curated gateway to Arabidopsis biology, research materials and communityNucleic Acids Research, 2003
- Predicting transmembrane protein topology with a hidden markov model: application to complete genomesJournal of Molecular Biology, 2001
- Gapped BLAST and PSI-BLAST: a new generation of protein database search programsNucleic Acids Research, 1997
- Prediction of complete gene structures in human genomic DNAJournal of Molecular Biology, 1997
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997