Referenced in: none

Automatically associated channels: Kv2.1

Title: Two forms of Vibrio cholerae O1 El Tor hemolysin derived from identical precursor protein.

Authors: H Ikigai, T Ono, T Nakae, H Otsuru, T Shimamura

Journal, date & volume: Biochim. Biophys. Acta, 1999 Jan 8 , 1415, 297-305

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/9889386

Abstract
Vibrio cholerae O1 grown in heart infusion broth produces two forms of El Tor hemolysin (ETH) monomers of 65 and 50 kDa. These monomers form several different sizes of mixed oligomers ranging from 180 to 280 kDa in the liposomal membranes. We found that the N-terminal amino acid sequences, NH2-Trp-Pro-Ala-Pro-Ala-Asn-Ser-Glu, of both the 65- and 50-kDa toxins were identical. We assumed, therefore, that the 65- and 50-kDa toxins were derivatives of the identical precursor protein and the 50-kDa protein was a truncated derivative of 65-kDa ETH. To substantiate this assumption, we treated the 260-kDa oligomer with trypsin and obtained a 190-kDa oligomer. This 190-kDa oligomer consisted of only the 50-kDa subunits. Both 260- and 190-kDa oligomers formed ion channels indistinguishable from each other in planar lipid bilayers. These results suggest that the essential part of the ETH in forming the membrane-damaging aggregate is a 50-kDa protein.