EXCRETION OF PUTRESCINE BY THE PUTRESCINE-ORNITHINE ANTIPORTER ENCODED BY THE POTE GENE OF ESCHERICHIA-COLI

被引:118
作者
KASHIWAGI, K [1 ]
MIYAMOTO, S [1 ]
SUZUKI, F [1 ]
KOBAYASHI, H [1 ]
IGARASHI, K [1 ]
机构
[1] CHIBA UNIV,FAC PHARMACEUT SCI,YAYOI CHO 1-33,CHIBA 263,JAPAN
关键词
POLYAMINE TRANSPORT; POTE PROTEIN;
D O I
10.1073/pnas.89.10.4529
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
Excretion of putrescine from Escherichia coli was assessed by measuring its uptake into inside-out membrane vesicles. The vesicles were prepared from wild-type E. coli or E. coli transformed with plasmids containing one of the three polyamine transport systems. The results indicate that excretion of putrescine is catalyzed by the putrescine transport protein, encoded by the potE gene located at 16 min on the E. coli chromosome. Loading of ornithine (or lysine) inside the vesicles was essential for the uptake of putrescine, indicating that the protein exchanges putrescine and ornithine (or lysine) by an antiport mechanism. The K(m) and V(max) values for the putrescine uptake by inside-out membrane vesicles were 73-mu-M and 0.82 nmol/min per mg of protein, respectively. The antiport protein (potE protein) also catalyzed putrescine-putrescine and ornithine-ornithine exchange. The transport activity was not disturbed by inhibitors of energy production such as KCN and carbonyl cyanide m-chlorophenylhydrazone. When intact E. coli was used instead of the inside-out membrane vesicles, excretion of putrescine was also catalyzed by the antiport protein in the presence of ornithine in the medium.
引用
收藏
页码:4529 / 4533
页数:5
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