The N-end rule: functions, mysteries, uses

Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12142-9. doi: 10.1073/pnas.93.22.12142.

Abstract

The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. Similar but distinct versions of the N-end rule operate in all organisms examined, from mammals to fungi and bacteria. In eukaryotes, the N-end rule pathway is a part of the ubiquitin system. I discuss the mechanisms and functions of this pathway, and consider its applications.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Acyltransferases / metabolism
  • Amidohydrolases / metabolism
  • Amino Acid Sequence*
  • Animals
  • Evolution, Molecular
  • Female
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / metabolism
  • Half-Life
  • Ligases / metabolism
  • Male
  • Mice
  • Models, Biological*
  • Models, Chemical*
  • Protein Conformation
  • Proteins / metabolism*
  • Proto-Oncogene Proteins c-mos / metabolism
  • Rabbits
  • Saccharomyces cerevisiae Proteins*
  • Ubiquitin-Protein Ligases*

Substances

  • Fungal Proteins
  • Proteins
  • Saccharomyces cerevisiae Proteins
  • Acyltransferases
  • UBR1 protein, S cerevisiae
  • Ubiquitin-Protein Ligases
  • Proto-Oncogene Proteins c-mos
  • Amidohydrolases
  • GTP-Binding Proteins
  • Ligases