Journal
BMC BIOINFORMATICS
Volume 15, Issue -, Pages -Publisher
BMC
DOI: 10.1186/1471-2105-15-222
Keywords
VASt; VAD1; Protein domain; Programmed cell death; GRAM domain; Bet v1-like
Categories
Funding
- TULIP [ANR-10-LABX-41]
- Marie Curie CIG grant [334036]
- European Research Council (ERC) [336808]
- European Research Council (ERC) [336808] Funding Source: European Research Council (ERC)
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Background: Several regulators of programmed cell death (PCD) in plants encode proteins with putative lipid-binding domains. Among them, VAD1 is a regulator of PCD propagation harboring a GRAM putative lipid-binding domain. However the function of VAD1 at the subcellular level is unknown and the domain architecture of VAD1 has not been analyzed in details. Results: We analyzed sequence conservation across the plant kingdom in the VAD1 protein and identified an uncharacterized VASt (VAD1 Analog of StAR-related lipid transfer) domain. Using profile hidden Markov models (profile HMMs) and phylogenetic analysis we found that this domain is conserved among eukaryotes and generally associates with various lipid-binding domains. Proteins containing both a GRAM and a VASt domain include notably the yeast Ysp2 cell death regulator and numerous uncharacterized proteins. Using structure-based phylogeny, we found that the VASt domain is structurally related to Bet v1-like domains. Conclusion: We identified a novel protein domain ubiquitous in Eukaryotic genomes and belonging to the Bet v1-like superfamily. Our findings open perspectives for the functional analysis of VASt-containing proteins and the characterization of novel mechanisms regulating PCD.
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