Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli

• Published in: Biophysical journal Vol. 73; no. 4; pp. 1925 - 1931
• Main Authors: Cruickshank, C.C., Minchin, R.F., Le Dain, A.C., Martinac, B.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.10.1997
• Subjects: Bacterial Proteins; Biophysical Phenomena; Biophysics; Electric Conductivity; Escherichia coli - metabolism; Ion Channel Gating; Ion Channels - chemistry; Ion Channels - metabolism; Models, Chemical; Permeability; Polyamines - metabolism; Space life sciences; Stress, Mechanical
• ISSN: 0006-3495; 1542-0086
• DOI: 10.1016/S0006-3495(97)78223-7

The open channel diameter of Escherichia coli recombinant large-conductance mechanosensitive ion channels (MscL) was estimated using the model of Hille (Hille, B. 1968. Pharmacological modifications of the sodium channels of frog nerve. J. Gen. Physiol. 51:199–219) that relates the pore size to conductance. Based on the MscL conductance of 3.8 nS, and assumed pore lengths, a channel diameter of 34 to 46 A was calculated. To estimate the pore size experimentally, the effect of large organic ions on the conductance of MscL was examined. Poly-L-lysines (PLLs) with a diameter of 37 A or larger significantly reduced channel conductance, whereas spermine (approximately 15 A), PLL19 (approximately 25 A) and 1,1'-bis-(3-(1'-methyl-(4,4'-bipyridinium)-1-yl)-propyl)-4,4'-b ipyridinium (approximately 30 A) had no effect. The smaller organic ions putrescine, cadaverine, spermine, and succinate all permeated the channel. We conclude that the open pore diameter of the MscL is approximately 40 A, indicating that the MscL has one of the largest channel pores yet described. This channel diameter is consistent with the proposed homohexameric model of the MscL.