BACTERIAL LEADER PEPTIDASE, A MEMBRANE-PROTEIN WITHOUT A LEADER PEPTIDE, USES THE SAME EXPORT PATHWAY AS PRE-SECRETORY PROTEINS

被引：84

作者：

WOLFE, PB ^{[1
]}

WICKNER, W ^{[1
]}

机构：

[1] UNIV CALIF LOS ANGELES,DEPT BIOL CHEM,LOS ANGELES,CA 90024

来源：

CELL | 1984年 / 36卷 / 04期

关键词：

D O I：

10.1016/0092-8674(84)90056-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：1067 / 1072

页数：6

共 42 条

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[2] BRUSILOW WSA, 1981, J BIOL CHEM, V256, P3141
[3] ROLE FOR MEMBRANE-POTENTIAL IN THE SECRETION OF PROTEIN INTO THE PERIPLASM OF ESCHERICHIA-COLI
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[5] MECHANISMS OF MEMBRANE ASSEMBLY - EFFECTS OF ENERGY POISONS ON THE CONVERSION OF SOLUBLE M13-COLIPHAGE PROCOAT TO MEMBRANE-BOUND COAT PROTEIN
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[6] DAUM G, 1982, J BIOL CHEM, V257
[7] INVITRO AND INVIVO PRODUCTS OF ESCHERICHIA-COLI LACTOSE PERMEASE GENE ARE IDENTICAL
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[8] ENERGY IS REQUIRED FOR MATURATION OF EXPORTED PROTEINS IN ESCHERICHIA-COLI
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[J]. CELL, 1981, 23 (02) : 411 - 422
[10] IMPORTED MITOCHONDRIAL PROTEINS CYTOCHROME-B2 AND CYTOCHROME-C1 ARE PROCESSED IN 2 STEPS
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