Biomaterial Database

Recognition of the 3' terminus of 2'-O-aminoacyl transfer ribonucleic acid by the acceptor site of ribosomal peptidyltransferase. 1975

D Ringer, and K Quiggle, and S Chládek

The interaction of the 3' terminus of 2'- and 3'-O-aminoacyl-tRNA with the peptidyltransferase A site of Escherichia coli ribosomes has been studied using the following aminoacyl oligonucleotides as models of the 3' terminus of AA-tRNA: C-A-Phe, C-A(2'Phe)H, C-A(2'H)Phe, C-A(2'Phe)Me, C-A(2'Me)Phe, C-A(2'Gly)H, and C-A(2'H)Gly. The transfer of Ac-(14C)Phe from the Ac-(14C)Phe-tRNA-oly(U)-70S ribosome complex to puromycin (10-4 and 10-5 M) was inhibited by C-A-Phe, C-A(2'Phe)H, C-A(2'H)Phe, C-A(2'Gly)H, and C-A(2'H)Gly. Kinetic analysis of the inhibition of Ac(14C)Phe-puromycin formation by C-A(2'Phe)H failed to show simple competitive inhibition. Binding of C-A-C-C-A-(14C)Phe to 70S ribosomes in the presence of an excess of deacylated tRNA was also inhibited by C-A-Phe, C-A(2'Phe)H, C-A(2'H)Phe, C-A(2'Phe)Me, and C-A(2'Me)Phe. It appears that the acceptor site of peptidyltransferase can recognize the 3' terminus of either 2'- or 3'-O-AA-tRNA, with preference for the 2' isomer. It therefore follows that 2'-O-AA-tRNA amy be bound to ribosomes prior to peptide bone formation and that 3'-O-AA-tRNA, which is used exclusively by peptidyltransferase as an acceptor, is supplied by 2' leads to 3' transacylation occuring at the peptidyltransferase A site.

UI	MeSH Term	Description	Entries
D009690	Nucleic Acid Conformation	The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.	DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D009841	Oligonucleotides	Polymers made up of a few (2-20) nucleotides. In molecular genetics, they refer to a short sequence synthesized to match a region where a mutation is known to occur, and then used as a probe (OLIGONUCLEOTIDE PROBES). (Dorland, 28th ed)	Oligonucleotide
D010445	Peptide Elongation Factors	Protein factors uniquely required during the elongation phase of protein synthesis.	Elongation Factor,Elongation Factors, Peptide,Factor, Elongation,Factors, Peptide Elongation
D010452	Peptide Biosynthesis	The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.	Biosynthesis, Peptide
D010649	Phenylalanine	An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.	Endorphenyl,L-Phenylalanine,Phenylalanine, L-Isomer,L-Isomer Phenylalanine,Phenylalanine, L Isomer
D011072	Poly U	A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties.	Polyuridylic Acids,Uracil Polynucleotides,Poly(rU),Acids, Polyuridylic,Polynucleotides, Uracil
D011691	Puromycin	A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis.	CL-13900,P-638,Puromycin Dihydrochloride,Puromycin Hydrochloride,Stylomycin,CL 13900,CL13900,P 638,P638
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000217	Acyltransferases	Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.	Acyltransferase
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining