Back to Search
Start Over
Substrate specificity of ribosomal peptidyl transferase. II. 2′(3′)-O-Aminoacyl nucleosides as acceptors of the peptide chain in the fragment reaction
- Source :
- Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis. 204:203-209
- Publication Year :
- 1970
- Publisher :
- Elsevier BV, 1970.
-
Abstract
- Transfer of the acetyl- l -leucine (AcLeu) residue from AcLeu-pentanucleotide to synthetic substrates under conditions of the fragment reaction was used to study the specificity of the acceptor site of ribosomal peptidyl transferase. 2′(3′)-O-Aminoacyl nucleosides are the simplest acceptor substrates. Their acceptor activity is dependent on the nature of the nucleoside to which the amino acid residue is bound. The acceptor activity decreased in the sequence 2′(3′)-O- l -phenylalanyladenosine (A-(Phe)) > I-(Phe) > C-(Phe); U-(Phe) was inactive. The presence of a free 2′-hydroxyl group in the ribose moiety of the aminoacyl adenosines was important for the acceptor activity, as shown by the low activity of dA-(Phe) in comparison with A-(Phe). Acceptor activity was influenced by the nature of the side chain of the amino acid residue bound to adenosine: A-(Phe) was a more active acceptor than puromycin, while the acceptor activity of 2′(3′)-O-glycyladenosine A-(Gly) was very low. Free phenylalanine, phenylalanine methyl ester, and adenosine did not act as acceptors. As terminal products of the reactions of AcLeu-pentanucleotide with puromycin, A-(Phe), I-(Phe) and C-(Phe), we isolated AcLeu-puromycin, 2′(3′)-O- acetyl- l -leucyl- l -phenylalanyladenosine (A-(AcLeu-Phe)), I-(AcLeu-Phe) and C-(AcLeu-Phe), respectively.
- Subjects :
- Electrophoresis
Paper
Peptide Biosynthesis
Peptidyl transferase
Chemical Phenomena
Stereochemistry
Phenylalanine
Peptide
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Residue (chemistry)
RNA, Transfer
Leucine
Transferases
Escherichia coli
Nucleotide
chemistry.chemical_classification
Carbon Isotopes
Binding Sites
biology
Nucleotides
Nucleosides
Acceptor
Chemistry
RNA, Bacterial
chemistry
biology.protein
Puromycin
Nucleoside
Subjects
Details
- ISSN :
- 00052787
- Volume :
- 204
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis
- Accession number :
- edsair.doi.dedup.....1d755c7a681c30f37c2e2a8c362a8df9