A HYDROPHOBIC REGION OF RICIN-A-CHAIN WHICH MAY HAVE A ROLE IN MEMBRANE TRANSLOCATION CAN FUNCTION AS AN EFFICIENT NONCLEAVED SIGNAL PEPTIDE

被引：10

作者：

CHADDOCK, JA ^{[1
]}

ROBERTS, LM ^{[1
]}

JUNGNICKEL, B ^{[1
]}

LORD, JM ^{[1
]}

机构：

[1] HARVARD UNIV,SCH MED,DEPT CELL BIOL,BOSTON,MA 02115

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 217卷 / 01期

关键词：

D O I：

10.1006/bbrc.1995.2746

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：

Ricin A chain is a polypeptide of 267 amino acids containing a hydrophobic region near its carboxyl-terminus (residues 245-256) which has been implicated in the membrane translocation step necessary for this catalytically active toxin to reach its intracellular substrate. DNA fusions were constructed that encoded hybrid proteins consisting of carboxyl-terminal residues 233-267 or residues 238-267 of ricin A chain preceding mouse dihydrofolate reductase. When in vitro transcripts prepared from these constructs were translated in cell-free systems, the ricin A chain-derived sequences functioned as efficient signal peptides which directed dihydrofolate reductase into microsomes or into proteoliposomes containing microsomal membrane components. (C) 1995 Academic Press, Inc.

引用

页码：68 / 73

页数：6

共 20 条

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[2]

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