EFFECT OF COLICINS-IA AND COLICINS-E1 ON ION PERMEABILITY OF LIPOSOMES

被引:59
作者
TOKUDA, H [1 ]
KONISKY, J [1 ]
机构
[1] UNIV ILLINOIS,DEPT MICROBIOL,URBANA,IL 61801
关键词
D O I
10.1073/pnas.76.12.6167
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Colicins Ia and E1 are shown to inhibit the formation and bring about the collapse of a potassium diffusion potential imposed across the membrane of liposomes prepared from soybean or Escherichia coli phospholipids. Such depolarization results from a colicin-induced increase in membrane ion permeability. Colicins E2 and E3 do not depolarize such membranes. In addition to the colicin Ia-induced rapid efflux of preloaded rubidium, sodium phosphate, or choline from liposomes, a slower efflux of preloaded sucrose or glucose 6-phosphate occurs. However, treated liposomes do not leak inulin or dextran, demonstrating that the effects of E1 and Ia are not due to a general disruption of membrane structure. The fact that colicin-induced ion efflux is observed in the complete absence of a membrane potential shows that the action of these colicins on liposomes is not voltage dependent. These results provide strong evidence that the depolarization of E. coli cells by colicins Ia and E1 results from a colicin-induced increase in membrane permeability to ions. It is proposed that this is brought about by the direct interaction of the colicin molecules with the bacterial cytoplasmic membrane.
引用
收藏
页码:6167 / 6171
页数:5
相关论文
共 21 条
[1]   LIGHT-DRIVEN SODIUM-TRANSPORT IN SUB-BACTERIAL PARTICLES OF HALOBACTERIUM-HALOBIUM [J].
EISENBACH, M ;
COOPER, S ;
GARTY, H ;
JOHNSTONE, RM ;
ROTTENBERG, H ;
CAPLAN, SR .
BIOCHIMICA ET BIOPHYSICA ACTA, 1977, 465 (03) :599-613
[2]  
GILCHRIST MJR, 1975, J BIOL CHEM, V250, P2457
[3]  
GOULD JM, 1977, J BIOL CHEM, V252, P5491
[4]   ION TRANSFER ACROSS LIPID-MEMBRANES IN PRESENCE OF GRAMICIDIN-A .1. STUDIES OF UNIT CONDUCTANCE CHANNEL [J].
HLADKY, SB ;
HAYDON, DA .
BIOCHIMICA ET BIOPHYSICA ACTA, 1972, 274 (02) :294-&
[5]  
HOLLAND IB, 1975, ADV MICROB PHYSIOL, V12, P56
[6]  
Kaback HR, 1971, METHOD ENZYMOL, V22, P99, DOI DOI 10.1016/0076-6879(71)22015-2
[7]  
KASAHARA M, 1977, J BIOL CHEM, V252, P7384
[8]  
KAYALAR C, 1979, BACTERIOL P, P146
[9]  
KIMELBERG HK, 1971, J BIOL CHEM, V246, P1142
[10]  
KONISKY J, 1970, J BIOL CHEM, V245, P2972