ArticleGenome biology2004
Hidden localization motifs: naturally occurring peroxisomal targeting signals in non-peroxisomal proteins.
Article in Genome biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Computational Evaluation of Peroxisomal Targeting Signals in Metazoa.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Sharing the wealth: The versatility of proteins targeted to peroxisomes and other organelles.Frontiers in cell and developmental biology · 2022Review
- Insights Into the Peroxisomal Protein Inventory of Zebrafish.Frontiers in physiology · 2022Article
- Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.Proteomics · 2015Article
- Comprehensive proteomics analysis of glycosomes from Leishmania donovani.Omics : a journal of integrative biology · 2015Article
- The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance.Frontiers in physiology · 2015Review
- Leishmania donovani argininosuccinate synthase is an active enzyme associated with parasite pathogenesis.PLoS neglected tropical diseases · 2012Article
- Structural requirements for interaction of peroxisomal targeting signal 2 and its receptor PEX7.The Journal of biological chemistry · 2011Article
- Identification of novel plant peroxisomal targeting signals by a combination of machine learning methods and in vivo subcellular targeting analyses.The Plant cell · 2011Article
- OPA3, mutated in 3-methylglutaconic aciduria type III, encodes two transcripts targeted primarily to mitochondria.Molecular genetics and metabolism · 2010Article
- Prediction of disease-related mutations affecting protein localization.BMC genomics · 2009Article
- Role of an ancestral d-bifunctional protein containing two sterol-carrier protein-2 domains in lipid uptake and trafficking in Toxoplasma.Molecular biology of the cell · 2009Article
- Predicted mouse peroxisome-targeted proteins and their actual subcellular locations.BMC bioinformatics · 2008Article
- Towards complete sets of farnesylated and geranylgeranylated proteins.PLoS computational biology · 2007Article
- pkaPS: prediction of protein kinase A phosphorylation sites with the simplified kinase-substrate binding model.Biology direct · 2007Article
- Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes.Plant physiology · 2006Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCan sequence segments coding for subcellular targeting or for posttranslational modifications occur in proteins that are not substrates in either of these processes? Although considerable effort has been invested in achieving low false-positive prediction rates, even accurate sequence-analysis tools for the recognition of these motifs generate a small but noticeable number of protein hits that lack the appropriate biological context but cannot be rationalized as false positives.
resultsWe show that the carboxyl termini of a set of definitely non-peroxisomal proteins with predicted peroxisomal targeting signals interact with the peroxisomal matrix protein receptor peroxin 5 (PEX5) in a yeast two-hybrid test. Moreover, we show that examples of these proteins - chicken lysozyme, human tyrosinase and the yeast mitochondrial ribosomal protein L2 (encoded by MRP7) - are imported into peroxisomes in vivo if their original sorting signals are disguised. We also show that even prokaryotic proteins can contain peroxisomal targeting sequences.
conclusionsThus, functional localization signals can evolve in unrelated protein sequences as a result of neutral mutations, and subcellular targeting is hierarchically organized, with signal accessibility playing a decisive role. The occurrence of silent functional motifs in unrelated proteins is important for the development of sequence-based function prediction tools and the interpretation of their results. Silent functional signals have the potential to acquire importance in future evolutionary scenarios and in pathological conditions.
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