Ribosomal Features Essential for tna Operon Induction: Tryptophan Binding at the Peptidyl Transferase Center
نویسندگان
چکیده
منابع مشابه
Ribosomal features essential for tna operon induction: tryptophan binding at the peptidyl transferase center.
Features of the amino acid sequence of the TnaC nascent peptide are recognized by the translating ribosome. Recognition leads to tryptophan binding within the translating ribosome, inhibiting the termination of tnaC translation and preventing Rho-dependent transcription termination in the tna operon leader region. It was previously shown that inserting an adenine residue at position 751 or intr...
متن کامل23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction.
Distinct features of the ribosomal peptide exit tunnel are known to be essential for recognition of specific amino acids of a nascent peptidyl-tRNA. Thus, a tryptophan residue at position 12 of the peptidyl-tRNA TnaC-tRNA(Pro) leads to the creation of a free tryptophan binding site within the ribosome at which bound tryptophan inhibits normal ribosome functions. The ribosomal processes that are...
متن کاملThe ribosomal peptidyl transferase.
Peptide bond formation on the ribosome takes place in an active site composed of RNA. Recent progress of structural, biochemical, and computational approaches has provided a fairly detailed picture of the catalytic mechanism of the reaction. The ribosome accelerates peptide bond formation by lowering the activation entropy of the reaction due to positioning the two substrates, ordering water in...
متن کاملConserved Residues Asp16 and Pro24 of TnaC-tRNA Participate in Tryptophan Induction of tna Operon Expression
In Escherichia coli, interactions between the nascent TnaC-tRNA peptidyl-tRNA and the translating ribosome create a tryptophan binding site in the ribosome where bound tryptophan inhibits TnaC-tRNA cleavage. This inhibition delays ribosome release, thereby inhibiting Rho factor binding and action, resulting in increased tna operon transcription. Replacing Trp12 of TnaC with any other amino acid...
متن کاملConserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of Tna operon expression.
In Escherichia coli, interactions between the nascent TnaC-tRNA(Pro) peptidyl-tRNA and the translating ribosome create a tryptophan binding site in the ribosome where bound tryptophan inhibits TnaC-tRNA(Pro) cleavage. This inhibition delays ribosome release, thereby inhibiting Rho factor binding and action, resulting in increased tna operon transcription. Replacing Trp12 of TnaC with any other ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2007
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.01869-06