Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate

Regulation of mRNA translation elongation impacts nascent protein synthesis and integrity and plays a critical role in disease establishment. Here, we investigate features linking regulation of codon-dependent translation elongation to protein expression and homeostasis. Using knockdown models of enzymes that catalyze the mcm5s2 wobble uridine tRNA modification (U34-enzymes), we show that gene codon content is necessary but not sufficient to predict protein fate. While translation defects upon perturbation of U34-enzymes are strictly dependent on codon content, the consequences on protein output are determined by other features. Specific hydrophilic motifs cause protein aggregation and degradation upon codon-dependent translation elongation defects. Accordingly, the combination of codon content and the presence of hydrophilic motifs define the proteome whose maintenance relies on U34-tRNA modification. Together, these results uncover the mechanism linking wobble tRNA modification to mRNA translation and aggregation to maintain proteome homeostasis.

Is it possible for short peptide composed of positively- and negatively-charged “hydrophilic” amino acid residue-clusters to form metastable “hydrophobic” packing?

Hybrid electrostatic/hydrophobic contacts constitute metastable “hydrophobic” packing of an intrinsic disordered peptide (IDP) composed of “hydrophilic” residue clusters.

Enhanced adsorption performance of aspartic acid intercalated Mg-Zn-Fe-LDH materials for arsenite

Hydrophobic and hydrophilic amino acid intercalated layered double hydroxides were synthesized and evaluated, and Mg7-Zn1-Fe4-Asp-LDH exhibited high removal efficiency for arsenic.