NDLI: The NfeD Protein Family and Its Conserved Gene Neighbours Throughout Prokaryotes: Functional Implications for Stomatin-Like Proteins

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Evolutionary Analysis of Mammalian Enamelin, The Largest Enamel Protein, Supports a Crucial Role for the 32-kDa Peptide and Reveals Selective Adaptation in Rodents and Primates

The NfeD Protein Family and Its Conserved Gene Neighbours Throughout Prokaryotes: Functional Implications for Stomatin-Like Proteins

Journal of Molecular Evolution : Volume 69, Issue 5, November 2009

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Journal of Molecular Evolution : Volume 69, Issue 3, September 2009

Journal of Molecular Evolution : Volume 69, Issue 2, August 2009

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The NfeD Protein Family and Its Conserved Gene Neighbours Throughout Prokaryotes: Functional Implications for Stomatin-Like Proteins

Content Provider	Springer Nature Link
Author	Green, Jasper B. Lower, Ryan P. J. Young, J. Peter W.
Copyright Year	2009
Abstract	NfeD-like proteins are widely distributed throughout prokaryotes and are frequently associated with genes encoding stomatin-like proteins (slipins). Here, we reveal that the NfeD family is ancient and comprises three major groups: NfeD1a, NfeD1b and truncated NfeD1b. Members of each group are associated with one of four conserved gene partners, three of which have eukaryotic homologues that are membrane raft associated, namely stomatin, paraslipin (previously SLP-2) and flotillin. The first NfeD group (NfeD1b), comprises proteins of approximately 460-aa long that have three functional domains: an N-terminal protease, a middle membrane-spanning region and a soluble C-terminal region rich in β-strands. The nfeD1b gene is adjacent to eoslipin in prokaryotic genomes except in Firmicutes and Deinococci, where yqfA replaces eoslipin. Proteins in the second major group (NfeD1a) are homologous to the C-terminus of NfeD1b which forms a β-barrel-like domain, and their genes are associated with paraslipin. Using OrthoMCL clustering, we show that nfeD1b genes have become truncated on many independent occasions giving rise to the third major group. These short NfeD homologues frequently remain associated with their ancestral gene neighbour, resembling NfeD1a in structure, yet are much more related to full-length NfeD1b; we term these “truncated NfeD1b”. These conserved associations suggest that NfeD proteins are dependent on gene partners for their function and that the site of interaction may lie within the C-terminal portion that is common to all NfeD homologues. Although NfeD homologues are confined to prokaryotes, this conserved association could represent an excellent system to study slipin and flotillin proteins.
Starting Page	657
Ending Page	667
Page Count	11
File Format	PDF
ISSN	00222844
Journal	Journal of Molecular Evolution
Volume Number	69
Issue Number	6
e-ISSN	14321432
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-11-30
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	SPFH Eoslipin Paraslipin SLP-2 Stomatin Flotillin NfeD YqfA YqeZ Phylogeny Animal Genetics and Genomics Plant Genetics & Genomics Plant Sciences Microbiology Evolutionary Biology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Genetics Molecular Biology Ecology, Evolution, Behavior and Systematics

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