NDLI: The expanding superfamily of gelsolin homology domain proteins.

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The expanding superfamily of gelsolin homology domain proteins.

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The expanding superfamily of gelsolin homology domain proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ghoshdastider, Umesh Popp, David Burtnick, Leslie D. Robinson, Robert C.
Description	Country affiliation: Singapore Author Affiliation: Ghoshdastider U ( Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Biopolis, 138673, Singapore.)
Abstract	The gelsolin homology (GH) domain has been found to date exclusively in actin-binding proteins. In humans, three copies of the domain are present in CapG, five copies in supervillin, and six copies each in adseverin, gelsolin, flightless I and the villins: villin, advillin and villin-like protein. Caenorhabditis elegans contains a four-GH-domain protein, GSNL-1. These architectures are predicted to have arisen from gene triplication followed by gene duplication to result in the six-domain protein. The subsequent loss of one, two or three domains produced the five-, four-, and three-domain proteins, respectively. Here we conducted BLAST and hidden Markov based searches of UniProt and NCBI databases to identify novel gelsolin domain containing proteins. The variety in architectures suggests that the GH domain has been tested in many molecular constructions during evolution. Of particular note is flightless-like I protein (FLIIL1) from Entamoeba histolytica, which combines a leucine rich repeats (LRR) domain, seven GH domains, and a headpiece domain, thus combining many of the features of flightless I with those of villin or supervillin. As such, the GH domain superfamily appears to have developed along complex routes. The distribution of these proteins was analyzed in the 343 completely sequenced genomes, mapped onto the tree of life, and phylogenetic trees of the proteins were constructed to gain insight into their evolution. © 2013 Wiley Periodicals, Inc.
File Format	HTM / HTML
ISSN	19493584
Issue Number	11
Volume Number	70
e-ISSN	19493592
Journal	Cytoskeleton
Language	English
Publisher	Wiley
Publisher Date	2013-11-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Cell Biology Gelsolin Chemistry Multigene Family Sequence Homology, Amino Acid Actin Cytoskeleton Metabolism Amino Acid Sequence Animals Conserved Sequence Genome Genetics Humans Models, Molecular Molecular Sequence Data Phylogeny Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Structural Biology

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