| Literature DB >> 35188662 |
Lioba Inken Winckler1,2,3, Nico Dissmeyer4,5,6.
Abstract
Studying the stability of a protein dependent on its N-terminal residue requires a mechanism, which selectively exposes the amino acid at the N-terminus. Here, we describe the use of the tobacco etch virus (TEV) protease to generate a specific N-terminal amino acid in the stroma of the chloroplast. The established molecular reporter system further allows the quantification of the reporter protein half-life dependent on the identity of the N-terminal residue.Entities:
Keywords: Chloroplasts; N-degron pathway; Protein degradation; TEV protease
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Year: 2022 PMID: 35188662 DOI: 10.1007/978-1-0716-1791-5_10
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745