In vitro protein folding by E. coli ribosome: unfolded protein splitting 70S to interact with 50S subunit.
Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a "folding competent" state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.
Basu
Arunima
A
Department of Biophysics, Molecular Biology and Genetics, University College of Science, 92 A.P.C. Road, Kolkata 700009, India.
Samanta
Dibyendu
D
Das
Debasis
D
Chowdhury
Saheli
S
Bhattacharya
Arpita
A
Ghosh
Jaydip
J
Das
Anindita
A
Dasgupta
Chanchal
C
D001665:Binding Sites; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis / Q000502:physiology; D017510:Protein Folding; D021122:Protein Subunits; D054681:Ribosome Subunits, Large, Bacterial / Q000737:chemistry* / Q000378:metabolism*
D029968:Escherichia coli Proteins; D021122:Protein Subunits