Instruction of Translating Ribosome by Nascent Peptide

Expression of the tryptophanase operon of Escherichia coli is regulated by catabolite repression and trsyptophan-induced transcription antitermination. An induction site activated by L-tryptophan is created in the translating ribosome during synthesis of TnaC, the 24-residue leader peptide. Replacin...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2002-09, Vol.297 (5588), p.1864-1867
Main Authors: Gong, Feng, Yanofsky, Charles
Format: Article
Language:English
Subjects:
Aminoglycosides
Anti-Bacterial Agents - pharmacology
Bacteria
Bacterial Proteins - biosynthesis
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biological and medical sciences
Chloramphenicol - pharmacology
Coding
Codon
Codon, Terminator
Codons
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
Gene expression
Gene Expression Regulation, Bacterial
Gongs
Logical Thinking
Molecular and cellular biology
Molecular genetics
Operator regions
Operon
Operons
Peptide Chain Termination, Translational
Peptides
Peptidyl Transferases - metabolism
Protein Biosynthesis - drug effects
Reverse Transcriptase Polymerase Chain Reaction
Ribonucleic acid
Ribosomes
Ribosomes - metabolism
RNA
RNA, Bacterial - metabolism
RNA, Transfer - metabolism
RNA, Transfer, Amino Acyl - metabolism
Stop codon
Templates, Genetic
Terminator codon
Transfer RNA
Translation
Translation. Translation factors. Protein processing
Tryptophan
Tryptophan - analogs & derivatives
Tryptophan - metabolism
Tryptophan - pharmacology
Tryptophanase - biosynthesis
Tryptophanase - genetics
Tunnels
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Items that cite this one
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Description
Summary:Expression of the tryptophanase operon of Escherichia coli is regulated by catabolite repression and trsyptophan-induced transcription antitermination. An induction site activated by L-tryptophan is created in the translating ribosome during synthesis of TnaC, the 24-residue leader peptide. Replacing the tnaC stop codon with a tryptophan codon allows tryptophan-charged tryptophan transfer RNA to substitute for tryptophan as inducer. This suggests that the ribosomal A site occupied by the tryptophanyl moiety of the charged transfer RNA is the site of induction. The location of tryptophan-12 of nascent TnaC in the peptide exit tunnel was crucial for induction. These results show that a nascent peptide sequence can influence translation continuation and termination within a translating ribosome.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1073997