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Tytuł pozycji:

A d-Amino Acid at the N-Terminus of a Protein Abrogates Its Degradation by the N-End Rule Pathway.

Tytuł:
A d-Amino Acid at the N-Terminus of a Protein Abrogates Its Degradation by the N-End Rule Pathway.
Autorzy:
Rabideau AE; Department of Chemistry, Massachusetts Institute of Technology , 18-596, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.
Pentelute BL; Department of Chemistry, Massachusetts Institute of Technology , 18-596, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.
Źródło:
ACS central science [ACS Cent Sci] 2015 Nov 25; Vol. 1 (8), pp. 423-430. Date of Electronic Publication: 2015 Nov 11.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Original Publication: Washington DC : ACS Publications, [2015]-
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Grant Information:
U54 AI057159 United States AI NIAID NIH HHS
Entry Date(s):
Date Created: 20160126 Latest Revision: 20201001
Update Code:
20240104
PubMed Central ID:
PMC4711398
DOI:
10.1021/acscentsci.5b00308
PMID:
26807441
Czasopismo naukowe
Eukaryotes have evolved the ubiquitin (Ub)/proteasome system to degrade polypeptides. The Ub/proteasome system is one way that cells regulate cytosolic protein and amino acids levels through the recognition and ubiquitination of a protein's N-terminus via E1, E2, and E3 enzymes. The process by which the N-terminus stimulates intracellular protein degradation is referred to as the N-end rule. Characterization of the N-end rule has been limited to only the natural l-amino acids. Using a cytosolic delivery platform derived from anthrax lethal toxin, we probed the stability of mixed chirality proteins, containing one d-amino acid on the N-terminus of otherwise all l-proteins. In all cases, we observed that one N-terminal d-amino acid stabilized the cargo protein to proteasomal degradation with respect to the N-end rule. We found that since the mixed chirality proteins were not polyubiquitinated, they evaded N-end-mediated proteasomal degradation. Evidently, a subtle change on the N-terminus of a natural protein can enhance its intracellular lifetime.

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