Literature DB >> 35188662

Engineering Destabilizing N-Termini in Plastids.

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.
© 2022. Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Chloroplasts; N-degron pathway; Protein degradation; TEV protease

Mesh:

Substances:

Year:  2022        PMID: 35188662     DOI: 10.1007/978-1-0716-1791-5_10

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  2 in total

1.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

2.  The Arabidopsis Chloroplast Stromal N-Terminome: Complexities of Amino-Terminal Protein Maturation and Stability.

Authors:  Elden Rowland; Jitae Kim; Nazmul H Bhuiyan; Klaas J van Wijk
Journal:  Plant Physiol       Date:  2015-09-14       Impact factor: 8.340

  2 in total

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