Selected article for: "acceptor site and lysine residue"

Author: Shapira, Assaf; Benhar, Itai
Title: Toxin-Based Therapeutic Approaches
  • Document date: 2010_10_28
  • ID: 00cf294x_58
    Snippet: The half-lives of proteins in a living cell range from a few seconds to many days. Features of proteins that confer metabolic instability are called degradation signals, or degrons. The N-end rule degron (N-degron), which was the first to be discovered, relates the in vivo half-life of a protein to the identity of its amino-terminal residue. In eukaryotes, the N-degron comprises at least two determinants: a destabilizing N-terminal residue and in.....
    Document: The half-lives of proteins in a living cell range from a few seconds to many days. Features of proteins that confer metabolic instability are called degradation signals, or degrons. The N-end rule degron (N-degron), which was the first to be discovered, relates the in vivo half-life of a protein to the identity of its amino-terminal residue. In eukaryotes, the N-degron comprises at least two determinants: a destabilizing N-terminal residue and internal lysine/s that function as acceptor site/s for the formation of a multi-ubiquitin chain that "marks" the ubiquitin-protein conjugates as a substrate for proteosomal degradation. Destabilizing residues in mammalian cells can be hierarchically divided into three classes: Primary (type 1 (Arg, Lys or His) or type 2 (Ile, Leu, Phe, Tyr or Trp)), secondary (Asp, Glu or oxidized Cys) and tertiary (Asn, Gln or Cys) (reviewed in [506] [507] [508] [509] [510] [511] ).

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