title: tRNA concentration fine tunes protein solubility.
abstract: Clusters of codons pairing to low-abundance tRNAs synchronize the translation with co-translational folding of single domains in multidomain proteins. Although proven with some examples, the impact of the ribosomal speed on the folding and solubility on a global, cell-wide level remains elusive. Here we show that upregulation of three low-abundance tRNAs in Escherichia coli increased the aggregation propensity of several cellular proteins as a result of an accelerated elongation rate. Intriguingly, alterations in the concentration of the natural tRNA pool compromised the solubility of various chaperones consequently rendering the solubility of some chaperone-dependent proteins.
authors: Institute of Biochemistry and Biology, University of Potsdam, Potsdam, Germany.
authors: Ivan
authors: I
authors: Fedyunin
authors: Lothar
authors: L
authors: Lehnhardt
authors: Nadine
authors: N
authors: Böhmer
authors: Paul
authors: P
authors: Kaufmann
authors: Gong
authors: G
authors: Zhang
authors: Zoya
authors: Z
authors: Ignatova
mesh_terms: D003062:Codon / Q000235:genetics / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010441:Peptide Chain Elongation, Translational; D017510:Protein Folding; D055503:Protein Multimerization; D012329:RNA, Bacterial / Q000235:genetics / Q000378:metabolism*; D012343:RNA, Transfer / Q000235:genetics / Q000378:metabolism*; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D003062:Codon; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D012329:RNA, Bacterial; D012343:RNA, Transfer