Aspartate-phobia of thermophiles as a reaction to deleterious chemical transformations

Bioessays. 2022 Jan;44(1):e2100213. doi: 10.1002/bies.202100213. Epub 2021 Nov 17.

Abstract

Prokaryotes growing at high temperatures have a high proportion of charged residues in their proteins to stabilize their 3D structure. By mining 175 disparate bacterial and archaeal proteomes we found that, against the general trend for charged residues, the frequency of aspartic acid residues decreases strongly as natural growth temperature increases. In search of the explanation, we hypothesized that the reason for such unusual correlation is the deleterious consequences of spontaneous chemical transformations of aspartate at high temperatures. Our subsequent statistical analysis supported this hypothesis. This finding reveals that organisms have likely adapted to high temperatures by minimizing the harmful consequences of spontaneous chemical transformations.

Keywords: aspartic acid; evolution; intrinsically disordered regions; protein conformation; spontaneous chemical reactions; statistical analysis; thermophiles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea
  • Aspartic Acid*
  • Bacteria / genetics
  • Bacterial Proteins
  • Humans
  • Phobic Disorders*
  • Proteome

Substances

  • Bacterial Proteins
  • Proteome
  • Aspartic Acid