Scientific article
Open access

Protein Abundance Biases the Amino Acid Composition of Disordered Regions to Minimize Non-functional Interactions

Published inJournal of Molecular Biology, vol. 431, no. 24, p. 4978-4992
Publication date2019-12

In eukaryotes, disordered regions cover up to 50% of proteomesR = − 0.55. Beyond this global amino-acid composition bias, we identify three rules by which amino-acid composition of disordered regions adjusts with high abundance. First, lysines are preferred over arginines, consistent with the latter amino acid being stickier than the former. Second, compensatory effects exist, whereby a sticky region can be tolerated if it is compensated by a distal non-sticky region. Third, such compensation requires a lower average stickiness at the same abundance when compared to a scenario where stickiness is homogeneous throughout the sequence. We validate these rules experimentally, employing them as different strategies to rescue an otherwise sticky protein fragment from aggregation. Our results highlight that non-functional interactions represent a significant constraint in cellular systems and reveal simple rules by which protein sequences adapt to that constraint.

  • Aggregation
  • Disordered regions
  • Intrinsic disorder
  • Non-functional interactions
  • Protein abundance
Affiliation Not a UNIGE publication
  • Israel Science Foundation -
  • European Research Council -
Citation (ISO format)
DUBREUIL, Benjamin, MATALON, Or, LEVY, Emmanuel. Protein Abundance Biases the Amino Acid Composition of Disordered Regions to Minimize Non-functional Interactions. In: Journal of Molecular Biology, 2019, vol. 431, n° 24, p. 4978–4992. doi: 10.1016/j.jmb.2019.08.008
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Article (Published version)
ISSN of the journal0022-2836

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