Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat synaptobrevin 2.
Tetanus toxin and the botulinum neurotoxins types A to F inhibit neurotransmitter release from presynaptic nerve endings by selectively proteolysing the synaptic proteins synaptobrevin, syntaxin, or SNAP-25. Here, we show that botulinum toxin type G cleaves rat synaptobrevin 2 between Ala81 and Ala82, a peptide bond that differs from those attacked by tetanus toxin and the botulinal toxins types B, D, and F. Synaptobrevin isoforms carrying a Gly in the P1 position are poor substrates. Analyses of N-terminal deletion mutants of rat synaptobrevin 2 showed that a substrate starting at Leu54 is cleaved efficiently, whereas substrates beginning at Leu60 or Phe77 are cleaved partially or not at all, respectively.
Yamasaki
S
S
Department of Microbiology, Federal Research Center for Virus Diseases of Animals, Tübingen, FRG.
Binz
T
T
Hayashi
T
T
Szabo
E
E
Yamasaki
N
N
Eklund
M
M
Jahn
R
R
Niemann
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D001905:Botulinum Toxins / Q000737:chemistry / Q000235:genetics / Q000633:toxicity*; D017931:DNA Primers / Q000235:genetics; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000633:toxicity; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D018377:Neurotransmitter Agents / Q000378:metabolism; D011487:Protein Conformation; D050683:R-SNARE Proteins; D051381:Rats; D017384:Sequence Deletion; D013379:Substrate Specificity; D013572:Synaptic Vesicles / Q000187:drug effects / Q000502:physiology
D017931:DNA Primers; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D018377:Neurotransmitter Agents; D050683:R-SNARE Proteins; D010450:Endopeptidases; D001905:Botulinum Toxins