Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Translocation of globin fusion proteins across the endoplasmic reticulum membrane in Xenopus laevis oocytes.
Simon K
,
Perara E
,
Lingappa VR
.
Abstract
We have studied the translocation of a normally cytoplasmic protein domain across the membrane of the endoplasmic reticulum in cell-free systems and in Xenopus laevis oocytes. Coding regions for the normally cytoplasmic protein globin were engineered in frame either 3' or 5' to the coding region for the signal sequence of either Escherichia coli b-lactamase or bovine preprolactin, respectively, in SP6 expression plasmids. RNA transcribed from these plasmids was microinjected into oocytes as well as translated in cell-free systems. We demonstrate that both in vivo and in vitro, a previously amino-terminal signal sequence can direct translocation of domains engineered to either side. Moreover, the domain preceding the signal sequence can be as large as that which follows it. While, in general, cell-free systems were found to faithfully reflect translocation events in vivo, our results suggest that a mechanism for clearance of signal peptides after cleavage is present in intact cells that is not reconstituted in cell-free systems.
Blobel,
Intracellular protein topogenesis.
1980, Pubmed
Blobel,
Intracellular protein topogenesis.
1980,
Pubmed
Colman,
The influence of topology and glycosylation on the fate of heterologous secretory proteins made in Xenopus oocytes.
1981,
Pubmed
,
Xenbase
Contreras,
Simple, efficient in vitro synthesis of capped RNA useful for direct expression of cloned eukaryotic genes.
1982,
Pubmed
,
Xenbase
Gilmore,
Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.
1982,
Pubmed
Gilmore,
Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation.
1983,
Pubmed
Gurdon,
Use of frog eggs and oocytes for the study of messenger RNA and its translation in living cells.
1971,
Pubmed
,
Xenbase
Hansen,
In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor.
1986,
Pubmed
Hortin,
Inhibition of preprotein processing in ascites tumor lysates by incorporation of a leucine analog.
1980,
Pubmed
Lingappa,
Determinants for protein localization: beta-lactamase signal sequence directs globin across microsomal membranes.
1984,
Pubmed
Lingappa,
Nascent prehormones are intermediates in the biosynthesis of authentic bovine pituitary growth hormone and prolactin.
1977,
Pubmed
Merrick,
Translation of exogenous mRNAs in reticulocyte lysates.
1983,
Pubmed
Meyer,
Secretory protein translocation across membranes-the role of the "docking protein'.
1982,
Pubmed
Meyer,
Signal recognition particle (SRP) does not mediate a translational arrest of nascent secretory proteins in mammalian cell-free systems.
1985,
Pubmed
Morgan,
Insulin action is blocked by a monoclonal antibody that inhibits the insulin receptor kinase.
1986,
Pubmed
,
Xenbase
Perara,
A former amino terminal signal sequence engineered to an internal location directs translocation of both flanking protein domains.
1985,
Pubmed
Perara,
Uncoupling translocation from translation: implications for transport of proteins across membranes.
1986,
Pubmed
Richter,
Differential capacity for translation and lack of competition between mRNAs that segregate to free and membrane-bound polysomes.
1981,
Pubmed
,
Xenbase
Siegel,
Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane.
1985,
Pubmed
Siegel,
Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact.
,
Pubmed
Tabe,
Segregation of mutant ovalbumins and ovalbumin-globin fusion proteins in Xenopus oocytes. Identification of an ovalbumin signal sequence.
1984,
Pubmed
,
Xenbase
Valle,
Anti-ovalbumin monoclonal antibodies interact with their antigen in internal membranes of Xenopus oocytes.
1982,
Pubmed
,
Xenbase
Walter,
Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.
1981,
Pubmed
Walter,
Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum.
1980,
Pubmed
Walter,
Preparation of microsomal membranes for cotranslational protein translocation.
1983,
Pubmed
Walter,
Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.
1981,
Pubmed
Waters,
Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis.
1986,
Pubmed
