Folding of the MS2 coat protein in Escherichia coli is modulated by translational pauses resulting from mRNA secondary structure and codon usage: a hypothesis.
Possible translational pauses within the coat protein of the RNA bacteriophage MS2 were located on the basis of a distribution plot of rare codons and RNA secondary structure. It appeared that the position of certain codon pauses corresponds with the size of some nascent polypeptide intermediates, which have been isolated from MS2-infected cells. Other accumulated polypeptide intermediates seemed to be related to RNA regions, where double-stranded secondary structures occur, which probably impede the movement of ribosomes during chain elongation. We assume that a discontinuous translation rate is designed to allow optimal folding of this (and other) polypeptide(s).
Guisez
Y
Y
Laboratory of Molecular Biology, Gent University, Belgium.
Robbens
J
J
Remaut
E
E
Fiers
W
W
D002213:Capsid / Q000235:genetics*; D036022:Capsid Proteins; D003062:Codon / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D008957:Models, Genetic; D008968:Molecular Conformation; D014176:Protein Biosynthesis / Q000235:genetics*; D017433:Protein Structure, Secondary; D012333:RNA, Messenger / Q000235:genetics*; D016601:RNA-Binding Proteins
D036022:Capsid Proteins; D003062:Codon; D012333:RNA, Messenger; D016601:RNA-Binding Proteins