Abstract
Targeting of vesicles to the acceptor membrane in protein transport depends on membrane proteins called SNAREs. Saccharomyces cerevisiae Golgi t-SNARE Sed5 protein and its neural cognate syntaxin 1 have similar three alpha-helices which are predicted to form coiled coils. We dissected the helices of Sed5 and found several characteristics unexpectedly distinct from those of syntaxin 1. Most importantly, only the N-terminal helix is responsible for the binding of Sly1 protein while almost the entire molecule of syntaxin is necessary for the binding of the cognate, Munc-18. The N-terminal region of Sed5 protein also binds to the C-terminal helix and Sly1 protein interfered this binding.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Antigens, Surface / chemistry
-
Antigens, Surface / genetics
-
Antigens, Surface / metabolism*
-
Cell Membrane / metabolism
-
Golgi Apparatus / metabolism*
-
Membrane Proteins / chemistry
-
Membrane Proteins / genetics
-
Membrane Proteins / metabolism*
-
Nerve Tissue Proteins / chemistry
-
Nerve Tissue Proteins / genetics
-
Nerve Tissue Proteins / metabolism*
-
Protein Binding
-
Protein Folding
-
Qa-SNARE Proteins
-
Recombinant Fusion Proteins / chemistry
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / metabolism
-
Saccharomyces cerevisiae / metabolism*
-
Saccharomyces cerevisiae / ultrastructure
-
Saccharomyces cerevisiae Proteins*
-
Syntaxin 1
Substances
-
Antigens, Surface
-
Membrane Proteins
-
Nerve Tissue Proteins
-
Qa-SNARE Proteins
-
Recombinant Fusion Proteins
-
Saccharomyces cerevisiae Proteins
-
Sed5 protein, S cerevisiae
-
Syntaxin 1