Association of the components of the binary toxin from Bacillus sphaericus in solution and with model lipid bilayers.
We show herein that interaction in aqueous solution of the two components of binary toxin from Bacillus sphaericus, BinA and BinB, leads to a dramatic conformational change, from beta turns or random coil, to beta structure. Also, either BinA or BinB separately or their equimolar mixture, interact with lipid bilayers resulting in further conformational changes. Upon membrane association, the change in conformation observed for BinA or BinB separately is different from that observed when the proteins are combined, indicating that proper folding depends on the presence of the complementary subunit. We also show, in contrast to previous reports, that BinB, but not BinA, is able to insert in model neutral lipid monolayers.
Boonserm
Panadda
P
Institute of Molecular Biology and Genetics, Mahidol University, Salaya, Phuttamonthol, Nakornpathom 73170, Thailand. mbpbs@mahidol.ac.th
Moonsom
Seangduen
S
Boonchoy
Chanikarn
C
Promdonkoy
Boonhiang
B
Parthasarathy
Krupakar
K
Torres
Jaume
J
D001427:Bacterial Toxins / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions
D001427:Bacterial Toxins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D012996:Solutions; C046134:binB protein, Bacillus sphaericus