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

F. Laurent, G. Labesse, P. de Wit

Research output: Contribution to journalArticleAcademicpeer-review

39 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)286-292
JournalBiochemical and Biophysical Research Communications
Volume270
DOIs
Publication statusPublished - 2000

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