Disorderness in Escherichia coli proteome: perception of folding fidelity and protein-protein interactions.
Traditionally biased usage of synonymous codons renders selective advantage to proteins expressed at high levels with a few exceptions like in Escherichia coli. Proteome-wide characteristics indicative of trends in highly expressed proteins of E. coli is analyzed in this communication. Implications for the nature of interactions performed by these two groups of highly expressed proteins are discussed here. The group of highly expressed proteins having optimized codon usage through employment of most abundant tRNAs is already shielded from misfolding by their improved error-prone translational machinery. Our data also provide evidence for mechanism by which a significant proportion of highly expressed proteins with high intrinsic disorder evade degradation and successfully carry out their function.
Bioinformatics Centre, Bose Institute, P 1/12, C.I.T. Scheme VII M, Kolkata 700 054, India.
Bratati
B
Kahali
Tapash Chandra
TC
Ghosh
D003062:Codon; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D008954:Models, Biological; D017510:Protein Folding; D060066:Protein Interaction Maps; D020543:Proteome / Q000235:genetics / Q000378:metabolism*; D018709:Statistics, Nonparametric
D003062:Codon; D029968:Escherichia coli Proteins; D020543:Proteome