TY - JOUR
T1 - A chemical mapping technique for exploring the location of proteins along the ribosome-bound peptide chain
AU - Eilat, Dan
AU - Pellegrini, Maria
AU - Oen, Helen
AU - Lapidot, Yehuda
AU - Cantor, Charles R.
PY - 1974/10/5
Y1 - 1974/10/5
N2 - A series of peptidyl-tRNA analogs with varying peptide chain length, BrAc(Gly) nPhe-tRNAphe, n = 0 to 16 has been prepared. When bound to Escherichia coli 70 S ribosomes these all react covalently with certain ribosomal proteins. The overwhelming majority of the reaction is with 50 S ribosomal proteins L2, L16, L24, L26-L27 and L32-L33. The extent of reaction with each protein is a function of peptide chain length, making it possible to estimate the relative proximity of these proteins to the 3′-terminus of tRNA bound in the ribosomal P site. This fact, coupled with the findings of others about the length dependence of the binding and peptide donor activity of peptidyl-tRNAs suggests that there is actually a binding site for the growing peptide chain. If this is true, the results presented here permit the ordering of the proteins in this site: L2 is closest to the 3′-end of tRNA followed by L26-L27, L32-L33 and last L24. Evidence is also given that the direction of the growing peptide chain must point away from the A site.
AB - A series of peptidyl-tRNA analogs with varying peptide chain length, BrAc(Gly) nPhe-tRNAphe, n = 0 to 16 has been prepared. When bound to Escherichia coli 70 S ribosomes these all react covalently with certain ribosomal proteins. The overwhelming majority of the reaction is with 50 S ribosomal proteins L2, L16, L24, L26-L27 and L32-L33. The extent of reaction with each protein is a function of peptide chain length, making it possible to estimate the relative proximity of these proteins to the 3′-terminus of tRNA bound in the ribosomal P site. This fact, coupled with the findings of others about the length dependence of the binding and peptide donor activity of peptidyl-tRNAs suggests that there is actually a binding site for the growing peptide chain. If this is true, the results presented here permit the ordering of the proteins in this site: L2 is closest to the 3′-end of tRNA followed by L26-L27, L32-L33 and last L24. Evidence is also given that the direction of the growing peptide chain must point away from the A site.
UR - http://www.scopus.com/inward/record.url?scp=0016139120&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(74)90402-1
DO - 10.1016/0022-2836(74)90402-1
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C2 - 4610160
AN - SCOPUS:0016139120
SN - 0022-2836
VL - 88
SP - 831
EP - 840
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 4
ER -