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Structures of yeast vesicle trafficking proteins
Author(s) -
Tishgarten Tomer,
Yin Fang Fang,
Grant Tracy R.,
Lipscomb Leigh Ann,
Faucher Keith M.,
Dluhy Richard A.,
Stevens Tom H.,
Mollard Gabriele Fischer Von
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.11.2465
Subject(s) - snare complex , exocytosis , biology , vesicle fusion , yeast , vesicular transport protein , lipid bilayer fusion , vesicle , vesicular transport proteins , rab , protein structure , syntaxin , microbiology and biotechnology , synaptic vesicle , biochemistry , saccharomyces cerevisiae , membrane , gtpase , vacuolar protein sorting
In protein transport between organelles, interactions of v‐ and t‐SNARE proteins are required for fusion of proteincontaining vesicles with appropriate target compartments. Mammalian SNARE proteins have been observed to interact with NSF and SNAP, and yeast SNAREs with yeast homologues of NSF and SNAP proteins. This observation led to the hypothesis that, despite low sequence homology, SNARE proteins are structurally similar among eukaryotes. SNARE proteins can be classified into two groups depending on whether they interact with SNARE binding partners via conserved glutamine (Q‐SNAREs) or arginine (R‐SNAREs). Much of the published structural data available is for SNAREs involved in exocytosis (either in yeast or synaptic vesicles). This paper describes circular dichroism, Fourier transform infrared spectroscopy, and dynamic light scattering data for a set of yeast v‐ and t‐SNARE proteins, Vti 1p and Pep12p, that are Q‐SNAREs involved in intracellular trafficking. Our results suggest that the secondary structure of Vti1p is highly α‐helical and that Vti 1p forms multimers under a variety of solution conditions. In these respects, Vti1p appears to be distinct from R‐SNARE proteins characterized previously. The α‐helicity of Vti1p is similar to that of Q‐SNARE proteins characterized previously. Pep12p, a Q‐SNARE, is highly α‐helical. It is distinct from other Q‐SNAREs in that it forms dimers under many of the solution conditions tested in our experiments. The results presented in this paper are among the first to suggest heterogeneity in the functioning of SNARE complexes.