Jun 29, 2009 · In this paper, we present an analysis of characterized NLSs in yeast, and find, despite the large number of nuclear import pathways, that NLSs seem to show similar patterns of amino acid residues. We test current prediction methods and observe a low true positive rate.

By systematic amino acid replacement analyses in budding yeast, we created activity-based profiles for different classes of importin-α-dependent NLSs that represent the functional contributions of different amino acids at each position within an NLS class.

A nuclear localization signal or sequence (NLS) is an amino acid sequence that 'tags' a protein for import into the cell nucleus by nuclear transport. [1] Typically, this signal consists of one or more short sequences of positively charged lysines or arginines exposed on the protein surface. [1]

In this report, using fluorescence microscopy studies combined with mutational and functional analyses, I show that the yeast SmB and SmD1 NLS-like motifs exhibit nuclear localization properties.

The experiment results on the newly curated Yeast and Hybrid datasets show that SeqNLS is effective in detecting potential NLSs. The performance comparison between SeqNLS with and without the linear motif scoring shows that linear motif features are highly complementary to sequence features in discerning NLSs.

Short stretches of amino acids, termed nuclear localization sequences (NLS), can mediate assembly of proteins into the nucleus. Proteins from the yeast, Saccharomyces cerevisiae, have been identified that specifically recognize nuclear localization peptides (Silver, P., I. Sadler, and M. A. Osborne. 1989. J. Cell Biol. 109:983-989).

In this study, we demonstrated that Ty1 IN indeed has a bipartite nuclear localization signal (NLS) that is essential for retrotransposition. This NLS differs from other bipartite signals in its long spacer region.

Sep 7, 2015 · Prokaryotic recombinases, CRISPR-associated proteins such as Cas9 or bacterial and viral polymerases require efficient NLSs to function in eukaryotes. The yeast Pichia pastoris is a widely used expression platform for heterologous protein production, but molecular tools such as NLSs are limited.

Plasmid 416Gal-SV40NLS-FUS-YFP from Dr. Aaron Gitler's lab contains the insert NLS-FUS and is published in PLoS Biol. 2011 Apr;9 (4):e1000614. doi: 10.1371/journal.pbio.1000614.

We have developed a simple genetic assay to detect active nuclear localization (NLS) and export signals (NES) on the basis of their function within yeast cells. The bacterial LexA protein was...