Protein folding following synthesis in vitro and in vivo: association of newly synthesized protein with 50S subunit of E. coli ribosome.
In the accompanying paper, it was shown that a protein, while reverting to native form from the unfolded state in vitro with the help of bacterial 70S ribosome, split the latter into its subunits (50S and 30S) and remains associated with the 50S subunit. Here, we follow the fate of nascent proteins both in case of in vivo and in vitro translation system. The newly synthesised protein was found to associate with the 50S subunit in both the cases.
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
Bhattacharya
Arpita
A
Das
Anindita
A
Das
Debasis
D
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