Catalytic roles of the AMP at the 3' end of tRNAs.
Recent reports suggest that the ribosome retains considerable peptidyl transferase activity even when much of the protein of the ribosome is removed and further suggests that rRNA may be the peptidyl transferase. The work here suggests that the AMP residue at the 3' terminus of each tRNA has some catalytic activity both in the esterification reaction and in forming a pseudopeptide, AcGly, and further suggests that whatever peptidyl transferase is, it finds a cooperative substrate in the aminoacyl-AMP at the 3' terminus of tRNA.
Wickramasinghe
N S
NS
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham 35294.
Lacey
J C
JC
D000107:Acetylation; D000249:Adenosine Monophosphate / Q000378:metabolism*; D002384:Catalysis; D003838:Deoxyadenine Nucleotides / Q000378:metabolism*; D004951:Esterification; D005998:Glycine / Q000378:metabolism; D009842:Oligopeptides / Q000096:biosynthesis*; D010458:Peptidyl Transferases / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D046249:Transfer RNA Aminoacylation
D003838:Deoxyadenine Nucleotides; D009842:Oligopeptides; D012346:RNA, Transfer, Amino Acyl; D000249:Adenosine Monophosphate; C012873:2'-deoxy-5'-adenosine monophosphate; D010458:Peptidyl Transferases; D005998:Glycine