TY - JOUR
T1 - Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA
AU - Green, Rachel
AU - Switzer, Christopher
AU - Noller, Harry F.
PY - 1998/4/10
Y1 - 1998/4/10
N2 - In the ribosome, the aminoacyl-transfer RNA (tRNA) analog 4-thio-dT-p- C-p-puromycin crosslinks photochemically with G2553 of 23S ribosomal RNA (rRNA). This covalently linked substrate reacts with a peptidyl-tRNA analog to form a peptide bond in a peptidyl transferase-catalyzed reaction. This result places the conserved 2555 loop of 23S rRNA at the peptidyl transferase A site and suggests that peptide bond formation can occur uncoupled from movement of the A-site tRNA. Crosslink formation depends on occupancy of the P site by a tRNA carrying an intact CCA acceptor end, indicating that peptidyl-tRNA, directly or indirectly, helps to create the peptidyl transferase A site.
AB - In the ribosome, the aminoacyl-transfer RNA (tRNA) analog 4-thio-dT-p- C-p-puromycin crosslinks photochemically with G2553 of 23S ribosomal RNA (rRNA). This covalently linked substrate reacts with a peptidyl-tRNA analog to form a peptide bond in a peptidyl transferase-catalyzed reaction. This result places the conserved 2555 loop of 23S rRNA at the peptidyl transferase A site and suggests that peptide bond formation can occur uncoupled from movement of the A-site tRNA. Crosslink formation depends on occupancy of the P site by a tRNA carrying an intact CCA acceptor end, indicating that peptidyl-tRNA, directly or indirectly, helps to create the peptidyl transferase A site.
UR - http://www.scopus.com/inward/record.url?scp=0032502997&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032502997&partnerID=8YFLogxK
U2 - 10.1126/science.280.5361.286
DO - 10.1126/science.280.5361.286
M3 - Article
C2 - 9535658
AN - SCOPUS:0032502997
SN - 0036-8075
VL - 280
SP - 286
EP - 289
JO - Science
JF - Science
IS - 5361
ER -