BOTULINUM NEUROTOXIN TYPE-C CLEAVES A SINGLE LYS-ALA BOND WITHIN THE CARBOXYL-TERMINAL REGION OF SYNTAXINS

被引：227
作者：
SCHIAVO, G
SHONE, CC
BENNETT, MK
SCHELLER, RH
MONTECUCCO, C
机构：
[1] UNIV PADUA,DIPARTIMENTO SCI BIOMED,I-35121 PADUA,ITALY
[2] PUBL HLTH LAB SERV,CTR APPL MICROBIOL & RES,PROT TOXINS SECT,SALISBURY SP4 0JG,WILTS,ENGLAND
[3] UNIV CALIF BERKELEY,DEPT MOLEC & CELL BIOL,BERKELEY,CA 94720
[4] STANFORD UNIV,HOWARD HUGHES MED INST,DEPT CELLULAR & MOLEC PHYSIOL,STANFORD,CA 94305
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 1995年 / 270卷 / 18期
关键词：
D O I：
10.1074/jbc.270.18.10566
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Botulinum neurotoxin serotype C (BoNT/C) is a 150-kDa protein produced by Clostridium botulinum, which causes animal botulism. In contrast to the other botulinum neurotoxins that contain one atom of zinc, highly purified preparations of BoNT/C bind two atoms of zinc per toxin molecule. BoNT/C is a zinc endopeptidase that cleaves syntaxin 1A at the Lys(253)-Ala(254) and syntaxin 1B at the Lys(252)-Ala(253) peptide bonds, only when they are inserted into a lipid bilayer. The other Lys-Ala bond present within the carboxyl-terminal region is not hydrolyzed. Syntaxin isoforms 2 and 3 are also cleaved by BoNT/C, while syntaxin 4 is resistant. These data suggest that BoNT/C recognizes a specific spatial organization of syntaxin, adopted upon membrane insertion, which brings a selected Lys-Ala peptide bond of its carboxyl-terminal region to the active site of this novel metalloproteinase.
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收藏
页码：10566 / 10570
页数：5
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