ArticleThe Journal of biological chemistry2014
Non-repair pathways for minimizing protein isoaspartyl damage in the yeast Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Bioinformatics of cyanophycin metabolism genes and characterization of promiscuous isoaspartyl dipeptidases that catalyze the final step of cyanophycin degradation.Scientific reports · 2023Article
- Directed Evolution of Aerotolerance in Sulfide-Dependent Thiazole Synthases.ACS synthetic biology · 2023Article
- Human Protein-l-isoaspartateBiochemistry · 2022Article
- l-Isoaspartyl Methyltransferase Deficiency in Zebrafish Leads to Impaired Calcium Signaling in the Brain.Frontiers in genetics · 2020Article
- The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.The Journal of biological chemistry · 2019Article
- Functional divergence of annotated l-isoaspartateThe Journal of biological chemistry · 2019Article
- Monocyte adhesion to atherosclerotic matrix proteins is enhanced by Asn-Gly-Arg deamidation.Scientific reports · 2017Article
- RNA-binding protein PSPC1 promotes the differentiation-dependent nuclear export of adipocyte RNAs.The Journal of clinical investigation · 2017Article
- Trans-membrane Signaling in Photosynthetic State Transitions: REDOX- AND STRUCTURE-DEPENDENT INTERACTION IN VITRO BETWEEN STT7 KINASE AND THE CYTOCHROME b6f COMPLEX.The Journal of biological chemistry · 2016Article
- (p)ppGpp-Dependent Persisters Increase the Fitness of Escherichia coli Bacteria Deficient in Isoaspartyl Protein Repair.Applied and environmental microbiology · 2016Article
- Deuteration protects asparagine residues against racemization.Amino acids · 2016Article
- Racemized and Isomerized Proteins in Aging Rat Teeth and Eye Lens.Rejuvenation research · 2016Article
- Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5.Amino acids · 2016Article
- The X-Linked-Intellectual-Disability-Associated Ubiquitin Ligase Mid2 Interacts with Astrin and Regulates Astrin Levels to Promote Cell Division.Cell reports · 2016Article
- Enzymatic attributes of an l-isoaspartyl methyltransferase fromBiochemistry and biophysics reports · 2015Article
- Prediction of Spontaneous Protein Deamidation from Sequence-Derived Secondary Structure and Intrinsic Disorder.PloS one · 2015Article
- Tctex1d2 associates with short-rib polydactyly syndrome proteins and is required for ciliogenesis.Cell cycle (Georgetown, Tex.) · 2015Article
- Article
- DUSP7 regulates the activity of ERK2 to promote proper chromosome alignment during cell division.The Journal of biological chemistryArticle
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4 authors.
Funding
Abstract
The spontaneous degradation of asparaginyl and aspartyl residues to isoaspartyl residues is a common type of protein damage in aging organisms. Although the protein-l-isoaspartyl (d-aspartyl) O-methyltransferase (EC 2.1.1.77) can initiate the repair of l-isoaspartyl residues to l-aspartyl residues in most organisms, no gene homolog or enzymatic activity is present in the budding yeast Saccharomyces cerevisiae. Therefore, we used biochemical approaches to elucidate how proteins containing isoaspartyl residues are metabolized in this organism. Surprisingly, the level of isoaspartyl residues in yeast proteins (50-300 pmol of isoaspartyl residues/mg of protein extract) is comparable with organisms with protein-l-isoaspartyl (d-aspartyl) O-methyltransferase, suggesting a novel regulatory pathway. Interfering with common protein quality control mechanisms by mutating and inhibiting the proteasomal and autophagic pathways in vivo did not increase isoaspartyl residue levels compared with wild type or uninhibited cells. However, the inhibition of metalloproteases in in vitro aging experiments by EDTA resulted in an ∼3-fold increase in the level of isoaspartyl-containing peptides. Characterization by mass spectrometry of these peptides identified several proteins involved in metabolism as targets of isoaspartyl damage. Further analysis of these peptides revealed that many have an N-terminal isoaspartyl site and originate from proteins with short half-lives. These results suggest that one or more metalloproteases participate in limiting isoaspartyl formation by robust proteolysis.
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