In vivo half-life of a protein is a function of its amino-terminal residue. Export

@article{citeulike:4159047, abstract = {When a chimeric gene encoding a ubiquitin-beta-galactosidase fusion protein is expressed in the yeast Saccharomyces cerevisiae, ubiquitin is cleaved off the nascent fusion protein, yielding a deubiquitinated beta-galactosidase (beta gal). With one exception, this cleavage takes place regardless of the nature of the amino acid residue of beta gal at the ubiquitin-beta gal junction, thereby making it possible to expose different residues at the amino-termini of the otherwise identical beta gal proteins. The beta gal proteins thus designed have strikingly different half-lives in vivo, from more than 20 hours to less than 3 minutes, depending on the nature of the amino acid at the amino-terminus of beta gal. The set of individual amino acids can thus be ordered with respect to the half-lives that they confer on beta gal when present at its amino-terminus (the "N-end rule"). The currently known amino-terminal residues in long-lived, noncompartmentalized intracellular proteins from both prokaryotes and eukaryotes belong exclusively to the stabilizing class as predicted by the N-end rule. The function of the previously described posttranslational addition of single amino acids to protein amino-termini may also be accounted for by the N-end rule. Thus the recognition of an amino-terminal residue in a protein may mediate both the metabolic stability of the protein and the potential for regulation of its stability.}, author = {Bachmair, A. and Finley, D. and Varshavsky, A.}, citeulike-article-id = {4159047}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/3018930}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=3018930}, day = {10}, issn = {0036-8075}, journal = {Science (New York, N.Y.)}, keywords = {n-end-rule-pathway, protein\_degradation}, month = {October}, number = {4773}, pages = {179--186}, posted-at = {2009-03-10 13:34:03}, priority = {2}, title = {In vivo half-life of a protein is a function of its amino-terminal residue.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/3018930}, volume = {234}, year = {1986} }

TY - JOUR ID - citeulike:4159047 L3 - citeulike-article-id:4159047 N2 - When a chimeric gene encoding a ubiquitin-beta-galactosidase fusion protein is expressed in the yeast Saccharomyces cerevisiae, ubiquitin is cleaved off the nascent fusion protein, yielding a deubiquitinated beta-galactosidase (beta gal). With one exception, this cleavage takes place regardless of the nature of the amino acid residue of beta gal at the ubiquitin-beta gal junction, thereby making it possible to expose different residues at the amino-termini of the otherwise identical beta gal proteins. The beta gal proteins thus designed have strikingly different half-lives in vivo, from more than 20 hours to less than 3 minutes, depending on the nature of the amino acid at the amino-terminus of beta gal. The set of individual amino acids can thus be ordered with respect to the half-lives that they confer on beta gal when present at its amino-terminus (the "N-end rule"). The currently known amino-terminal residues in long-lived, noncompartmentalized intracellular proteins from both prokaryotes and eukaryotes belong exclusively to the stabilizing class as predicted by the N-end rule. The function of the previously described posttranslational addition of single amino acids to protein amino-termini may also be accounted for by the N-end rule. Thus the recognition of an amino-terminal residue in a protein may mediate both the metabolic stability of the protein and the potential for regulation of its stability. IS - 4773 JF - Science (New York, N.Y.) SN - 0036-8075 EP - 186 TI - In vivo half-life of a protein is a function of its amino-terminal residue. VL - 234 SP - 179 KW - n-end-rule-pathway KW - protein_degradation AU - Bachmair, A AU - Finley, D AU - Varshavsky, A PY - 1986/10/10/ UR - http://view.ncbi.nlm.nih.gov/pubmed/3018930 ER -