The circular bacteriocin, carnocyclin A, forms anion-selective channels in lipid bilayers
نویسندگان
چکیده
منابع مشابه
Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers.
Recombinant beta-toxin from Clostridium perfringens type C was found to increase the conductance of bilayer lipid membranes (BLMs) by inducing channel activity. The channels exhibited a distribution of conductances within the range of 10 to 380 pS, with the majority of the channels falling into two categories of conductance at 110 and 60 pS. The radii of beta-toxin pores found for the conductan...
متن کاملDiphtheria toxin forms transmembrane channels in planar lipid bilayers.
When exposed to a lipid bilayer, diphtheria toxin binds to it and forms transmembrane, voltage-dependent, anion-selective channels. The mean (+/- SD) conductance of these channels in asolectin membranes is 6.2 +/- 0.7 pmho (pS) in 0.2 M NaCl and 20 +/- 2 pmho in 1.0 M NaCl. The rate of channel formation depends on the pH in the toxin-containing compartment; it is very low at pH greater than 5.0...
متن کاملVpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers.
A small (96-aa) protein, virus protein R (Vpr), of human immunodeficiency virus type 1 contains one hydrophobic segment that could form a membrane-spanning helix. Recombinant Vpr, expressed in Escherichia coli and purified by affinity chromatography, formed ion channels in planar lipid bilayers when it was added to the cis chamber and when the trans chamber was held at a negative potential. The...
متن کاملBordetella pertussis major outer membrane porin protein forms small, anion-selective channels in lipid bilayer membranes.
The major outer membrane protein of molecular weight 40,000 (the 40K protein) of a virulent isolate of Bordetella pertussis was purified to apparent homogeneity. The purified protein formed an oligomer band (of apparent molecular weight 90,000) on sodium dodecyl sulfate-polyacrylamide gels after solubilization at low temperatures. The porin function of this protein was characterized by the blac...
متن کاملThe synthetic precursor specific region of pre-pro-parathyroid hormone forms ion channels in lipid bilayers.
We have used the chemically synthesized sequence of pre-pro-parathyroid hormone and several of its analogues to test the notion that the capacity of amphipathic peptides to aggregate in membranes and form ion-permeable channels correlates with their ability to function as signal sequences for secreted proteins. We found that pre-pro-parathyroid hormone (the signal sequence and pro-region of par...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2009
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2009.05.008