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Structures of yeast vesicle trafficking proteins.

Publication ,  Journal Article
Tishgarten, T; Yin, FF; Faucher, KM; Dluhy, RA; Grant, TR; Fischer von Mollard, G; Stevens, TH; Lipscomb, LA
Published in: Protein Sci
November 1999

In protein transport between organelles, interactions of v- and t-SNARE proteins are required for fusion of protein-containing 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, Vti1p and Pep12p, that are Q-SNAREs involved in intracellular trafficking. Our results suggest that the secondary structure of Vti1p is highly alpha-helical and that Vti1p forms multimers under a variety of solution conditions. In these respects, Vti1p appears to be distinct from R-SNARE proteins characterized previously. The alpha-helicity of Vti1p is similar to that of Q-SNARE proteins characterized previously. Pep12p, a Q-SNARE, is highly alpha-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.

Duke Scholars

Published In

Protein Sci

DOI

ISSN

0961-8368

Publication Date

November 1999

Volume

8

Issue

11

Start / End Page

2465 / 2473

Location

United States

Related Subject Headings

  • Vesicular Transport Proteins
  • Scattering, Radiation
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Recombinant Proteins
  • Qb-SNARE Proteins
  • Qa-SNARE Proteins
  • Protein Structure, Secondary
  • Protein Conformation
  • Molecular Sequence Data
 

Citation

APA
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ICMJE
MLA
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Tishgarten, T., Yin, F. F., Faucher, K. M., Dluhy, R. A., Grant, T. R., Fischer von Mollard, G., … Lipscomb, L. A. (1999). Structures of yeast vesicle trafficking proteins. Protein Sci, 8(11), 2465–2473. https://doi.org/10.1110/ps.8.11.2465
Tishgarten, T., F. F. Yin, K. M. Faucher, R. A. Dluhy, T. R. Grant, G. Fischer von Mollard, T. H. Stevens, and L. A. Lipscomb. “Structures of yeast vesicle trafficking proteins.Protein Sci 8, no. 11 (November 1999): 2465–73. https://doi.org/10.1110/ps.8.11.2465.
Tishgarten T, Yin FF, Faucher KM, Dluhy RA, Grant TR, Fischer von Mollard G, et al. Structures of yeast vesicle trafficking proteins. Protein Sci. 1999 Nov;8(11):2465–73.
Tishgarten, T., et al. “Structures of yeast vesicle trafficking proteins.Protein Sci, vol. 8, no. 11, Nov. 1999, pp. 2465–73. Pubmed, doi:10.1110/ps.8.11.2465.
Tishgarten T, Yin FF, Faucher KM, Dluhy RA, Grant TR, Fischer von Mollard G, Stevens TH, Lipscomb LA. Structures of yeast vesicle trafficking proteins. Protein Sci. 1999 Nov;8(11):2465–2473.

Published In

Protein Sci

DOI

ISSN

0961-8368

Publication Date

November 1999

Volume

8

Issue

11

Start / End Page

2465 / 2473

Location

United States

Related Subject Headings

  • Vesicular Transport Proteins
  • Scattering, Radiation
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Recombinant Proteins
  • Qb-SNARE Proteins
  • Qa-SNARE Proteins
  • Protein Structure, Secondary
  • Protein Conformation
  • Molecular Sequence Data