ArticleCellular and molecular life sciences : CMLS2020
Structural and functional analysis of "non-smelly" proteins.
Article in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- The cellular economy while crafting regulatory processes relies on protein intrinsic disorder: how and why precision comes at a cost in protein structure.Cell communication and signaling : CCS · 2025Review
- Liquid-liquid phase separation: an emerging perspective on the tumorigenesis, progression, and treatment of tumors.Frontiers in immunology · 2025Review
- A Few Charged Residues in Galectin-3's Folded and Disordered Regions Regulate Phase Separation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure.Protein science : a publication of the Protein Society · 2024Review
- Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins.Nature protocols · 2023Review
- Computational prediction of disordered binding regions.Computational and structural biotechnology journal · 2023Review
- Comparative evaluation of AlphaFold2 and disorder predictors for prediction of intrinsic disorder, disorder content and fully disordered proteins.Computational and structural biotechnology journal · 2023Article
- On the Evolutionary History of the Twenty Encoded Amino Acids.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Review
- Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions.Biomolecules · 2022Article
- The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA-binding proteins for liquid-liquid phase separation.Protein science : a publication of the Protein Society · 2022Article
- Liquid-liquid phase separation as an organizing principle of intracellular space: overview of the evolution of the cell compartmentalization concept.Cellular and molecular life sciences : CMLS · 2022Review
- Design and Analysis of a Mutant form of the Ice-Binding Protein from Choristoneura fumiferana.The protein journal · 2022Article
- IDPology of the living cell: intrinsic disorder in the subcellular compartments of the human cell.Cellular and molecular life sciences : CMLS · 2021Article
- Ribosome Evolution and Structural Capacitance.Frontiers in molecular biosciences · 2019Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
Abstract
Cysteine and aromatic residues are major structure-promoting residues. We assessed the abundance, structural coverage, and functional characteristics of the "non-smelly" proteins, i.e., proteins that do not contain cysteine residues (C-depleted) or cysteine and aromatic residues (CFYWH-depleted), across 817 proteomes from all domains of life. The analysis revealed that although these proteomes contained significant levels of the C-depleted proteins, with prokaryotes being significantly more enriched in such proteins than eukaryotes, the CFYWH-depleted proteins were relatively rare, accounting for about 0.05% of proteomes. Furthermore, CFYWH-depleted proteins were virtually never found in PDB. Depletion in cysteine and in aromatic residues was associated with the substantially increased intrinsic disorder levels across all domains of life. Archaeal and eukaryotic organisms with higher levels of the C-depleted proteins were shown to have higher levels of the intrinsic disorder and lower levels of structural coverage. We also showed that the "non-smelly" proteins typically did not independently fold into monomeric structures, and instead, they fold by interacting with nucleic acids as constituents of the ribosome and nucleosome complexes. They were shown to be involved in translation, transcription, nucleosome assembly, transmembrane transport, and protein folding functions, all of which are known to be associated with the intrinsic disorder. Our data suggested that, in general, structure of monomeric proteins is crucially dependent on the presence of cysteine and aromatic residues.
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