Abstract：
:The pathogenically important cholesterol-binding pore-forming bacterial "thiol-activated" toxins (TATs) are commonly believed to be monomeric in solution and to undergo a transition on membrane binding mediated by cholesterol to an oligomeric pore. We present evidence, gained through the application of a number of biochemical and biophysical techniques with associated modelling, that the TAT from Streptococcus pneumoniae, pneumolysin, is in fact able to self-associate in solution to form the same oligomeric structures. The weak interaction leading to solution oligomerization is manifested at low concentrations in a dimeric toxin form. The inhibition of toxin self-interaction by derivatization of the single cysteine residue in pneumolysin with the thiol-active agent dithio (bis)nitrobenzoic acid indicates that self-interaction is mediated by the fourth domain of the protein, which has a fold similar to other proteins known to self-associate. This interaction is thought to have implications for the understanding of mechanisms of pore formation and complement activation by pneumolysin.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Gilbert RJ,Rossjohn J,Parker MW,Tweten RK,Morgan PJ,Mitchell TJ,Errington N,Rowe AJ,Andrew PW,Byron Odoi
10.1006/jmbi.1998.2258subject
Has Abstractpub_date
1998-12-11 00:00:00pages
1223-37issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(98)92258-6journal_volume
284pub_type
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journal_title：Journal of molecular biology
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abstract：:The gal P2 promoter can be inactivated by point mutations located in the -10 hexamer sequence or immediately upstream from it. Mutations at either site reduce expression in vivo and prevent the formation, in vitro, of tight complexes with RNA polymerase that give a strong footprint and can initiate transcription. Howe...
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