Abstract:
:Porins are trimeric proteins in the outer membranes of Gram-negative bacteria. Several of them, among them matrix porin of Escherichia coli, form symmetrically voltage-gated ion channels in planar bilayers. Trimers exhibit negative resistance at potentials larger than +/- 90mV. Here we show that, after two pores within a trimer close irreversibly, the remaining third pore shows channel properties distinct from those observed in the trimer. This residual pore exhibits an asymmetric current-voltage dependence with a pronounced polarity-dependent shift toward low potentials and rates of channel-closing and opening that are one to two orders of magnitude faster than those observed for single channels in a reversibly voltage-dependent trimer. Rectification of single channels thus resembles that of a voltage-gated channel type observed in outer membrane patches of E.coli spheroblasts, hinting at the relevance of the phenomenon in vivo.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Buehler LK,Rosenbusch JPdoi
10.1006/bbrc.1993.1094subject
Has Abstractpub_date
1993-01-29 00:00:00pages
624-9issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(83)71094-6journal_volume
190pub_type
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