A HYDROPHOBIC REGION OF RICIN-A-CHAIN WHICH MAY HAVE A ROLE IN MEMBRANE TRANSLOCATION CAN FUNCTION AS AN EFFICIENT NONCLEAVED SIGNAL PEPTIDE
UNSPECIFIED. (1995) A HYDROPHOBIC REGION OF RICIN-A-CHAIN WHICH MAY HAVE A ROLE IN MEMBRANE TRANSLOCATION CAN FUNCTION AS AN EFFICIENT NONCLEAVED SIGNAL PEPTIDE. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 217 (1). pp. 68-73. ISSN 0006-291XFull text not available from this repository.
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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS|
|Publisher:||ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS|
|Official Date:||5 December 1995|
|Number of Pages:||6|
|Page Range:||pp. 68-73|
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