Molecular cloning and partial characterization of a plant VAP33 homologue with a major sperm protein domain.

In a search for proteins interacting with the resistance protein Cf9 from tomato, a new cDNA was cloned and characterized. Protein sequence database searches suggested that the 120 residue-N terminal domain of the encoded protein (named VAP27) is highly similar to the VAP33 protein family from animals, to uncharacterized plant proteins, and to a lower extent, to the major sperm protein (MSP) from nematodes. The second half of the protein is similar to VAMP and to the VAP33 N-terminus comprising a predicted coiled-coil region followed by a transmembrane segment. The sequence/structure comparison of VAP27 with the crystal structure of AsMSP1 from Ascaris suum, using molecular modeling with the threading method, suggested that the N-terminus of VAP27 does possess a MSP-like domain that might participate in the formation of a protein-protein network. The coiled-coil region of VAP27 was modeled based on the structure of the VAP- and VAMP-containing SNARE complex. The coiled-coil region might also be involved in protein-protein interactions similar to VAP-VAMP interactions. Copyright 2000 Academic Press.