Conserved signal peptide of Notch3 inhibits interaction with proteasome

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Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase

The general secretory pathway (Sec) and twin-arginine translocase (Tat) operate in parallel to export proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. Substrates are targeted to their respective machineries by N-terminal signal peptides that share a tripartite organization; however, Tat signal peptides harbor a conserved and almost invari...

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Conserved Signal Peptide Recognition Systems across the Prokaryotic Domains

The twin-arginine translocation (Tat) pathway is a protein targeting system found in bacteria, archaea, and chloroplasts. Proteins are directed to the Tat translocase by N-terminal signal peptides containing SRRxFLK "twin-arginine" amino acid motifs. The key feature of the Tat system is its ability to transport fully folded proteins across ionically sealed membranes. For this reason the Tat pat...

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Characterisation of the Trichinella spiralis Deubiquitinating Enzyme, TsUCH37, an Evolutionarily Conserved Proteasome Interaction Partner

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ژورنال

عنوان ژورنال: Biochemical and Biophysical Research Communications

سال: 2007

ISSN: 0006-291X

DOI: 10.1016/j.bbrc.2007.01.151