ArticleProtein science : a publication of the Protein Society2013
Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
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- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.Protein science : a publication of the Protein Society · 2023Article
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.bioRxiv : the preprint server for biology · 2023Article
- Intrinsically disordered regions that drive phase separation form a robustly distinct protein class.The Journal of biological chemistry · 2023Article
- An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.Protein science : a publication of the Protein Society · 2022Article
- Translation stalling proline motifs are enriched in slow-growing, thermophilic, and multicellular bacteria.The ISME journal · 2022Article
- Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins.The Journal of biological chemistry · 2021Article
- The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins.International journal of molecular sciences · 2021Article
- Structural and Energetic Characterization of the Denatured State from the Perspectives of Peptides, the Coil Library, and Intrinsically Disordered Proteins.Molecules (Basel, Switzerland) · 2021Review
- An Unbound Proline-Rich Signaling Peptide Frequently SamplesFrontiers in molecular biosciences · 2021Article
- Hidden dynamic signatures drive substrate selectivity in the disordered phosphoproteome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Impact of Heat on Coil Hydrodynamic Size Yields the Energetics of Denatured State Conformational Bias.The journal of physical chemistry. B · 2019Article
- Phosphorylation of TIP3 Aquaporins duringCells · 2019Article
- Deciphering GRINA/Lifeguard1: Nuclear Location, CaInternational journal of molecular sciences · 2019Review
- Concomitant disorder and high-affinity zinc binding in the human zinc- and iron-regulated transport protein 4 intracellular loop.Protein science : a publication of the Protein Society · 2019Article
- Sequence Reversal Prevents Chain Collapse and Yields Heat-Sensitive Intrinsic Disorder.Biophysical journal · 2018Article
- Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Proteins · 2017Article
- The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction.Journal of molecular biology · 2017Article
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4 authors.
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Abstract
Intrinsically disordered (ID) proteins function in the absence of a unique stable structure and appear to challenge the classic structure-function paradigm. The extent to which ID proteins take advantage of subtle conformational biases to perform functions, and whether signals for such mechanism can be identified in proteome-wide studies is not well understood. Of particular interest is the polyproline II (PII) conformation, suggested to be highly populated in unfolded proteins. We experimentally determine a complete calorimetric propensity scale for the PII conformation. Projection of the scale into representative eukaryotic proteomes reveals significant PII bias in regions coding for ID proteins. Importantly, enrichment of PII in ID proteins, or protein segments, is also captured by other PII scales, indicating that this enrichment is robustly encoded and universally detectable regardless of the method of PII propensity determination. Gene ontology (GO) terms obtained using our PII scale and other scales demonstrate a consensus for molecular functions performed by high PII proteins across the proteome. Perhaps the most striking result of the GO analysis is conserved enrichment (P < 10(-8) ) of phosphorylation sites in high PII regions found by all PII scales. Subsequent conformational analysis reveals a phosphorylation-dependent modulation of PII, suggestive of a conserved "tunability" within these regions. In summary, the application of an experimentally determined polyproline II (PII) propensity scale to proteome-wide sequence analysis and gene ontology reveals an enrichment of PII bias near disordered phosphorylation sites that is conserved throughout eukaryotes.
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