The nuclear localization sequence of the SV40 T antigen promotes transgene uptake and expression in zebrafish embryo nuclei

1996 ◽  
Vol 5 (6) ◽  
pp. 451-458 ◽  
Author(s):  
Philippe Collas ◽  
Harald Husebye ◽  
Peter Aleström
Keyword(s):  
Nuclear Localization ◽  
Zebrafish Embryo ◽  
T Antigen ◽  
Nuclear Localization Sequence ◽  
Sv40 T Antigen ◽  
Localization Sequence

The SV40 T antigen nuclear localization sequence enhances nuclear import of vector DNA in embryos of a crustacean (Litopenaeus schmitti)

Gene ◽  
2004 ◽  
Vol 337 ◽  
pp. 71-77 ◽  
Author(s):  
Amilcar Arenal ◽  
Rafael Pimentel ◽  
Carmen Garcı́a ◽  
Eulogio Pimentel ◽  
Peter Aleström
Keyword(s):  
Nuclear Localization ◽  
Nuclear Import ◽  
T Antigen ◽  
Nuclear Localization Sequence ◽  
Sv40 T Antigen ◽  
Localization Sequence ◽  
Vector Dna

The yeast nucleoporin Nsp1 binds nuclear localization sequences in vitro

1996 ◽  
Vol 74 (3) ◽  
pp. 363-372 ◽  
Author(s):  
Werner Barth ◽  
Ursula Stochaj
Keyword(s):  
Nuclear Localization ◽  
Specific Binding ◽  
T Antigen ◽  
Nuclear Localization Sequence ◽  
Nuclear Pore ◽  
Sv40 T Antigen ◽  
Nuclear Targeting ◽  
Nuclear Localization Sequences

Facilitated transport of proteins into the nucleus requires nuclear localization sequences (NLSs) be present in the protein destined for the nucleus. The specific binding of NLSs by components of the nuclear transport apparatus is essential for these targeting reactions. We now report that the yeast nucleoporin Nsp1 binds specifically nuclear localization sequences in vitro. This nucleoporin recognizes several NLSs that are functional for nuclear targeting in vivo, including the NLS of SV40 T-antigen and of the yeast transcription factor Gal4. Nsp1 is organized into three domains, and we have located NLS binding sites to the N-terminal portion and the middle repetitive region of the protein. For the interaction between the NLS of SV40 T-antigen and Nsp1, we obtained association constants of 1.2 × 107 M−1 and 5 × 107 M−1. An association constant of 5 × 107 M−1 was determined for NLS binding to the repetitive domain of Nsp1. We analyzed binding of Nsp1 and its domains to a mutant version of the NLS derived from SV40 T-antigen, which poorly functions for nuclear targeting in vivo. The affinity for the mutant signal was about two orders of magnitude lower than for the wild-type NLS.Key words: Nsp1, nuclear pore complex, nucleoporin, nuclear localization sequence, protein targeting, yeast.

scholarly journals Analysis of mutations in the putative nuclear localization sequence of interleukin-1β

1991 ◽  
Vol 280 (1) ◽  
pp. 111-116 ◽  
Author(s):  
S Grenfell ◽  
N Smithers ◽  
S Witham ◽  
A Shaw ◽  
P Graber ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Interleukin 1 ◽  
Simian Virus 40 ◽  
T Antigen ◽  
Nuclear Accumulation ◽  
Nuclear Localization Sequence ◽  
Target Cells ◽  
Wild Type ◽  
Receptor Mediated Endocytosis ◽  
Localization Sequence

Previous studies have shown that, after receptor-mediated endocytosis, interleukin-1 alpha (IL1 alpha) and interleukin-1 beta (IL1 beta) are translocated to the nucleus, where they appear to accumulate. It has been suggested that nuclear translocation may be involved in the biological responsiveness of target cells to IL1 stimulation. The human IL1 beta molecule contains a seven-amino-acid sequence (-Pro208-Lys-Lys-Lys-Met-Glu-Lys-) that shows some sequence identity with the nuclear localization sequence of the simian-virus-40 large T-antigen. The effects of point mutations within this putative nuclear localization sequence on IL1 beta binding, receptor-mediated endocytosis and biological activity have been characterized. Mutants M49 (Lys210→Ala), M50 (Lys211→Ala) and M51 (Pro208→Ala) all retained the ability to bind to the IL1 receptor, albeit with lower affinity than the wild-type molecules. However, mutants M49, M50 and M51 showed greater biological potency than wild-type IL1 alpha or IL1 beta, as measured by the induction of IL2 secretion. However, receptor-mediated endocytosis and nuclear accumulation of M50 were comparable with those in the wild-type. These observations suggest that the putative nuclear localization sequence may play an important role in the generation of biological responses to IL1 stimulation, even though it may not influence internalization of the ligand.

Luliberin analogues containing the nuclear localization sequence of the SV-40 virus T-antigen

2010 ◽  
Vol 36 (5) ◽  
pp. 581-588 ◽  
Author(s):  
S. V. Burov ◽  
T. V. Yablokova ◽  
M. Yu. Dorosh ◽  
E. V. Krivizyuk ◽  
A. M. Efremov ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
T Antigen ◽  
Nuclear Localization Sequence ◽  
Localization Sequence ◽  
Sv 40 Virus

scholarly journals Identification of the Nuclear Localization Signal inXenopus Cyclin E and Analysis of Its Role in Replication and Mitosis

2002 ◽  
Vol 13 (12) ◽  
pp. 4388-4400 ◽  
Author(s):  
Jonathan D. Moore ◽  
Sally Kornbluth ◽  
Tim Hunt
Keyword(s):  
Dna Replication ◽  
Nuclear Localization ◽  
Cyclin E ◽  
T Antigen ◽  
Cyclin B ◽  
Nuclear Accumulation ◽  
Nuclear Localization Sequence ◽  
Nuclear Targeting ◽  
Sv40 Large T Antigen ◽  
Localization Sequence

Cyclin-dependent kinase (Cdk)2/cyclin E is imported into nuclei assembled in Xenopus egg extracts by a pathway that requires importin-α and -β. Here, we identify a basic nuclear localization sequence (NLS) in the N-terminus ofXenopus cyclin E. Mutation of the NLS eliminated nuclear accumulation of both cyclin E and Cdk2, and such versions of cyclin E were unable to trigger DNA replication. Addition of a heterologous NLS from SV40 large T antigen restored both nuclear targeting of Cdk2/cyclin E and DNA replication. We present evidence indicating that Cdk2/cyclin E complexes must become highly concentrated within nuclei to support replication and find that cyclin A can trigger replication at much lower intranuclear concentrations. We confirmed that depletion of endogenous cyclin E increases the concentration of cyclin B necessary to promote entry into mitosis. In contrast to its inability to promote DNA replication, cyclin E lacking its NLS was able to cooperate with cyclin B in promoting mitotic entry.

scholarly journals Context affects nuclear protein localization in Saccharomyces cerevisiae.

1989 ◽  
Vol 9 (2) ◽  
pp. 384-389 ◽  
Author(s):  
M Nelson ◽  
P Silver
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Nuclear Localization ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Single Amino Acid ◽  
Nuclear Localization Sequence ◽  
Localization Sequence ◽  
Beta Galactosidase

Proteins destined for the nucleus contain nuclear localization sequences, short stretches of amino acids responsible for targeting them to the nucleus. We show that the first 29 amino acids of GAL4, a yeast DNA-binding protein, function efficiently as a nuclear localization sequence when fused to normally cytoplasmic invertase, but not when fused to Escherichia coli beta-galactosidase. Moreover, the nuclear localization sequence from simian virus 40 T antigen functions better when fused to invertase than when fused to beta-galactosidase. A single amino acid change in the T-antigen nuclear localization sequence inhibits the nuclear localization of simian virus 40-invertase and simian virus 40-beta-galactosidase in Saccharomyces cerevisiae. From these results, we conclude that the relative ability of a nuclear localization sequence to act depends on the protein to which it is linked.

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