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The effects of variations in the number and sequence of targeting signals on nuclear uptake.
Dworetzky SI
,
Lanford RE
,
Feldherr CM
.
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To determine if the number of targeting signals affects the transport of proteins into the nucleus, Xenopus oocytes were injected with colloidal gold particles, ranging in diameter from 20 to 280 A, that were coated with BSA cross-linked with synthetic peptides containing the SV-40 large T-antigen nuclear transport signal. Three BSA conjugate preparations were used; they had an average of 5, 8, and 11 signals per molecule of carrier protein. In addition, large T-antigen, which contains one signal per monomer, was used as a coating agent. The cells were fixed at various times after injection and subsequently analyzed by electron microscopy. Gold particles coated with proteins containing the SV-40 signal entered the nucleus through central channels located within the nuclear pores. Analysis of the intracellular distribution and size of the tracers that entered the nucleus indicated that the number of signals per molecule affect both the relative uptake of particles and the functional size of the channels available for translocation. In control experiments, gold particles coated with BSA or BSA conjugated with inactive peptides similar to the SV-40 transport signal were virtually excluded from the nucleus. Gold particles coated with nucleoplasmin, an endogenous karyophilic protein that contains five targeting signals per molecule, was transported through the nuclear pores more effectively than any of the BSA-peptide conjugates. Based on a correlation between the peri-envelope density of gold particles and their relative uptake, it is suggested that the differences in the activity of the two targeting signals is related to their binding affinity for envelope receptors. It was also determined, by performing coinjection experiments, that individual pores are capable of recognizing and transporting proteins that contain different nuclear targeting signals.
Bürglin,
The nuclear migration signal of Xenopus laevis nucleoplasmin.
1987, Pubmed,
Xenbase
Bürglin,
The nuclear migration signal of Xenopus laevis nucleoplasmin.
1987,
Pubmed
,
Xenbase
De Roe,
A model of protein-colloidal gold interactions.
1987,
Pubmed
Dingwall,
A polypeptide domain that specifies migration of nucleoplasmin into the nucleus.
1982,
Pubmed
,
Xenbase
Dingwall,
Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals.
1987,
Pubmed
,
Xenbase
Dumont,
Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals.
1972,
Pubmed
,
Xenbase
Dworetzky,
Translocation of RNA-coated gold particles through the nuclear pores of oocytes.
1988,
Pubmed
,
Xenbase
Feldherr,
Evidence for mediated protein uptake by amphibian oocyte nuclei.
1983,
Pubmed
Feldherr,
The uptake of endogenous proteins by oocyte nuclei.
1975,
Pubmed
,
Xenbase
Feldherr,
Movement of a karyophilic protein through the nuclear pores of oocytes.
1984,
Pubmed
,
Xenbase
FELDHERR,
THE EFFECT OF THE ELECTRON-OPAQUE PORE MATERIAL ON EXCHANGES THROUGH THE NUCLEAR ANNULI.
1965,
Pubmed
Goldfarb,
Synthetic peptides as nuclear localization signals.
,
Pubmed
,
Xenbase
Hall,
Targeting of E. coli beta-galactosidase to the nucleus in yeast.
1984,
Pubmed
Kalderon,
Sequence requirements for nuclear location of simian virus 40 large-T antigen.
,
Pubmed
Lanford,
Effect of basic and nonbasic amino acid substitutions on transport induced by simian virus 40 T-antigen synthetic peptide nuclear transport signals.
1988,
Pubmed
Lanford,
Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen.
1984,
Pubmed
Lanford,
Induction of nuclear transport with a synthetic peptide homologous to the SV40 T antigen transport signal.
1986,
Pubmed
Lyons,
Pentapeptide nuclear localization signal in adenovirus E1a.
1987,
Pubmed
Miller,
Artifacts caused by cell microinjection.
1984,
Pubmed
Moreland,
Identification of a nuclear localization signal of a yeast ribosomal protein.
1985,
Pubmed
Moreland,
Amino acid sequences that determine the nuclear localization of yeast histone 2B.
1987,
Pubmed
Newmeyer,
Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation.
1988,
Pubmed
,
Xenbase
Paine,
Nuclear envelope permeability.
1975,
Pubmed
Paine,
Nucleocytoplasmic movement of fluorescent tracers microinjected into living salivary gland cells.
1975,
Pubmed
Richardson,
Nuclear location signals in polyoma virus large-T.
1986,
Pubmed
Richardson,
Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores.
1988,
Pubmed
,
Xenbase
Roberts,
The effect of protein context on nuclear location signal function.
1987,
Pubmed
Silver,
Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization.
1984,
Pubmed
Simanis,
An immunoaffinity purification procedure for SV40 large T antigen.
1985,
Pubmed
Sugawa,
Foreign protein can be carried into the nucleus of mammalian cell by conjugation with nucleoplasmin.
1985,
Pubmed
,
Xenbase
