Abstract

Proteins of the SNARE (Soluble N-ethylmaleimide-sensitive factor attachment protein receptors) family play a significant role in all vesicular fusion events involved in endocytic and exocytic pathways. These proteins act as molecular machines that assemble into tight four-helix bundle complex, bridging the opposing membranes into close proximity forming membrane fusion. Almost all SNARE proteins share a 53 amino acid coiled-coil domain, which is mostly linked to the transmembrane domain at the C-terminal end. Despite significant variations between SNARE sequences across species, the SNARE mediated membrane fusion is evolutionary conserved in all eukaryotes. It is of interest to compare the functional divergence of SNARE proteins across various eukaryotic groups during evolution. Here, we report an exhaustive phylogeny of the SNARE proteins retrieved from SNARE database including plants, animals, fungi and protists. The Initial phylogeny segregated SNARE protein sequences into five well-supported clades Qa, Qb, Qc, Qbc and R reflective of their positions in the four-helix SNARE complex. Further to improve resolution the Qa, Qb, Qc and R family specific trees were reconstructed, each of these were further segregated into organelle specific clades at first and later diverged into lineage specific subgroups. This revealed that most of the SNARE orthologs are conserved at subcellular locations or at trafficking pathways across various species during eukaryotic evolution. The paralogous expansion in SNARE repertoire was observed at metazoans (animals) and plants independently during eukaryotic evolution. However, results also show that the multi-cellular and saprophytic fungi have limited SNAREs.

Highlights

  • A comprehensive phylogenetic analysis confirms that the basic Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) repertoire including twenty SNARE subgroups was conserved in Last eukaryotic common ancestor (LECA)

  • Persistent SNARE duplications were found in the endosomal and secretory pathways [14]. Many of these duplications in the Plasma membrane SNAREs lead to functional paralogs associated with differential kinetics of exocytosis especially in metazoans

  • These include the emergence of SNAP-23 (Slower kinetics of exocytosis) from SNAP-25; Syntaxin 2, 3, 4 from Syntaxin 1 and divergence of longins and brevins during eukaryotic evolution

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Summary

Introduction

An independent increase has been reported in the secretory and endocytic SNAREs in plants through detailed phylogenetic analysis [15]. This increase might be linked to the transition from unicellular to multicellular eukaryotic lifestyle. By contrast in depth phylogenetic survey in fungi suggested that multicellularity in fungi was achieved without an overall expansion in the SNARE repertoire [16]. Likewise many protists such as Paramecium harbor a large set of SNARE like proteins i.e., Synaptobrevin 8-12, SNAP-25 like as compared to flowering plants and metazoans [17].

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