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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Acyltransferases / metabolism
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Amidohydrolases / metabolism
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Amino Acid Sequence*
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Animals
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Evolution, Molecular
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Female
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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GTP-Binding Proteins / chemistry
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GTP-Binding Proteins / metabolism
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Half-Life
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Ligases / metabolism
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Male
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Mice
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Models, Biological*
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Models, Chemical*
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Protein Conformation
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Proteins / metabolism*
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Proto-Oncogene Proteins c-mos / metabolism
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Rabbits
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Saccharomyces cerevisiae Proteins*
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Ubiquitin-Protein Ligases*
Substances
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Fungal Proteins
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Proteins
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Saccharomyces cerevisiae Proteins
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Acyltransferases
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UBR1 protein, S cerevisiae
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Ubiquitin-Protein Ligases
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Proto-Oncogene Proteins c-mos
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Amidohydrolases
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GTP-Binding Proteins
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Ligases