The degradation signal in a short-lived protein
- PMID: 2538246
- DOI: 10.1016/0092-8674(89)90635-1
The degradation signal in a short-lived protein
Abstract
Our previous work has shown that the amino-terminal residue of a short-lived protein is a distinct component of the protein's degradation signal. To define the complete signal, otherwise identical dihydrofolate reductase test proteins bearing different extensions and either a "stabilizing" or a "destabilizing" amino-terminal residue were expressed in the yeast S. cerevisiae and their in vivo half-lives compared. The amino-terminal degradation signal is shown to comprise two distinct determinants. One, discovered previously, is the protein's amino-terminal residue. The second determinant, identified in the present work, is a specific lysine residue whose function in the degradation signal is not dependent on the unique amino acid sequences in the vicinity of the residue. The mechanistic significance of the second determinant is illuminated by the finding that in a targeted, short-lived protein, a chain of branched ubiquitin-ubiquitin conjugates is confined to a lysine residue that has been identified in the present work as the second determinant of the degradation signal.
Similar articles
-
The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo.Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4606-10. doi: 10.1073/pnas.88.11.4606. Proc Natl Acad Sci U S A. 1991. PMID: 1647011 Free PMC article.
-
A proteolytic pathway that recognizes ubiquitin as a degradation signal.J Biol Chem. 1995 Jul 21;270(29):17442-56. doi: 10.1074/jbc.270.29.17442. J Biol Chem. 1995. PMID: 7615550
-
Degradation signals in the lysine-asparagine sequence space.EMBO J. 1999 Nov 1;18(21):6017-26. doi: 10.1093/emboj/18.21.6017. EMBO J. 1999. PMID: 10545113 Free PMC article.
-
cis-trans recognition and subunit-specific degradation of short-lived proteins.Nature. 1990 Jul 19;346(6281):287-91. doi: 10.1038/346287a0. Nature. 1990. PMID: 2165217
-
The ubiquitin system for protein degradation.Annu Rev Biochem. 1992;61:761-807. doi: 10.1146/annurev.bi.61.070192.003553. Annu Rev Biochem. 1992. PMID: 1323239 Review. No abstract available.
Cited by
-
MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function.BMC Biochem. 2002 Sep 20;3:28. doi: 10.1186/1471-2091-3-28. BMC Biochem. 2002. PMID: 12370088 Free PMC article.
-
Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain.Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14110-5. doi: 10.1073/pnas.172527399. Epub 2002 Oct 21. Proc Natl Acad Sci U S A. 2002. PMID: 12391316 Free PMC article.
-
Structure-activity analysis of quorum-sensing signaling peptides from Streptococcus mutans.J Bacteriol. 2007 Feb;189(4):1441-50. doi: 10.1128/JB.00832-06. Epub 2006 Aug 25. J Bacteriol. 2007. PMID: 16936029 Free PMC article.
-
Crystal structure of a ubiquitin-dependent degradation substrate: a three-disulfide form of lysozyme.Proc Natl Acad Sci U S A. 1993 May 1;90(9):4136-40. doi: 10.1073/pnas.90.9.4136. Proc Natl Acad Sci U S A. 1993. PMID: 8387211 Free PMC article.
-
The substrate recognition domains of the N-end rule pathway.J Biol Chem. 2009 Jan 16;284(3):1884-95. doi: 10.1074/jbc.M803641200. Epub 2008 Nov 13. J Biol Chem. 2009. PMID: 19008229 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases