000133463 001__ 133463
000133463 005__ 20181203021431.0
000133463 0247_ $$2doi$$a10.1021/bi00151a026
000133463 037__ $$aARTICLE
000133463 245__ $$aSpectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proteolytic activation
000133463 269__ $$a1992
000133463 260__ $$c1992
000133463 336__ $$aJournal Articles
000133463 500__ $$aDepartment of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
000133463 520__ $$aThe channel-forming protein aerolysin is secreted as a protoxin which can be activated by proteolytic removal of a C-terminal peptide. The activation and subsequent oligomerization of aerolysin were studied using a variety of spectroscopic techniques. Mass spectrometric determination of the molecular weights of proaerolysin and aerolysin permitted identification of the sites at which the protoxin is processed by trypsin and chymotrypsin. The results of far- and near-UV circular dichroism measurements indicated that processing with trypsin does not lead to major changes in secondary or tertiary structure of the protein. An increase in tryptophan fluorescence intensity and a small red shift in the maximum emission wavelength of tryptophans could be observed, suggesting that there is a change in the environment of some of the tryptophans. There was also a dramatic increase in the binding of the hydrophobic fluorescent probe 1-anilino-8-naphthalenesulfonate during activation, leading us to conclude that a hydrophobic region in the protein is exposed by trypsin treatment. Using measurements of light scattering, various parameters influencing oligomerisation of trypsin-activated aerolysin were determined. Oligomerization rates were found to increase with the concentration of aerolysin, whereas they decreased with increasing ionic strength.
000133463 6531_ $$aAeromonas hydrophila/chemistry
000133463 6531_ $$aAmino Acid Sequence
000133463 6531_ $$aAnilino Naphthalenesulfonates/metabolism
000133463 6531_ $$aBacterial Toxins/*metabolism
000133463 6531_ $$aCircular Dichroism
000133463 6531_ $$aEndopeptidases/metabolism
000133463 6531_ $$aHemolysin Proteins/*physiology
000133463 6531_ $$aIon Channels/*physiology
000133463 6531_ $$aModels
000133463 6531_ $$aBiological
000133463 6531_ $$aMolecular Sequence Data
000133463 6531_ $$aPore Forming Cytotoxic Proteins
000133463 6531_ $$aProtein Conformation
000133463 6531_ $$aProtein Precursors/*metabolism
000133463 6531_ $$aSpectrometry
000133463 6531_ $$aFluorescence
000133463 6531_ $$aSpectrophotometry
000133463 6531_ $$aUltraviolet
000133463 6531_ $$aSubstrate Specificity
000133463 6531_ $$aTryptophan/chemistry
000133463 700__ $$0240085$$avan der Goot, F. G.$$g171549
000133463 700__ $$aLakey, J.
000133463 700__ $$aPattus, F.
000133463 700__ $$aKay, C. M.
000133463 700__ $$aSorokine, O.
000133463 700__ $$aVan Dorsselaer, A.
000133463 700__ $$aBuckley, J. T.
000133463 773__ $$j31$$k36$$q8566-70$$tBiochemistry
000133463 909C0 $$0252037$$pVDG$$xU11271
000133463 909CO $$ooai:infoscience.tind.io:133463$$pSV$$particle
000133463 937__ $$aVDG-ARTICLE-1992-004
000133463 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000133463 980__ $$aARTICLE