A Single Substitution in the Motif 1 of Escherichia coli Lysyl-tRNA Synthetase Induces Cooperativity toward Amino Acid Binding

Biochemistry ◽  
1995 ◽  
Vol 34 (25) ◽  
pp. 8180-8189 ◽  
Author(s):  
Stephane Commans ◽  
Sylvain Blanquet ◽  
Pierre Plateau
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Binding ◽  
Single Substitution

Substrate Specificity Is Determined by Amino Acid Binding Pocket Size in Escherichia coli Phenylalanyl-tRNA Synthetase

Biochemistry ◽  
1994 ◽  
Vol 33 (23) ◽  
pp. 7107-7112 ◽  
Author(s):  
Michael Ibba ◽  
Peter Kast ◽  
Hauke Hennecke
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Binding Pocket ◽  
Trna Synthetase ◽  
Amino Acid Binding

scholarly journals Transcription and translation in an RNA world

2006 ◽  
Vol 361 (1474) ◽  
pp. 1751-1760 ◽  
Author(s):  
William R Taylor
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Rna World ◽  
Large Subunit ◽  
Trna Synthetase ◽  
Nucleoside Triphosphate ◽  
Amino Acid Binding ◽  
World Hypothesis ◽  
Protein Elongation ◽  
Rna World Hypothesis

The RNA world hypothesis requires a ribozyme that was an RNA-directed RNA polymerase (ribopolymerase). If such a replicase makes a reverse complementary copy of any sequence (including itself), in a simple RNA world, there is no mechanism to prevent self-hybridization. It is proposed that this can be avoided through the synthesis of a parallel complementary copy. The logical consequences of this are pursued and developed in a computer simulation, where the behaviour of the parallel copy is compared to the conventional reverse complementary copy. It is found that the parallel copy is more efficient at higher temperatures (up to 90°C). A model for the ribopolymerase, based on the core of the large subunit (LSU) of the ribosome, is described. The geometry of a potential active site for this ribopolymerase suggests that it contained a cavity (now occupied by the aminoacyl-tRNA) and that an amino acid binding in this might have ‘poisoned’ the ribopolymerase by cross-reacting with the nucleoside-triphosphate before polymerization could occur. Based on a similarity to the active site components of the class-I tRNA synthetase enzymes, it is proposed that the amino acid could become attached to the nascent RNA transcript producing a variety of aminoacylated tRNA-like products. Using base-pairing interactions, some of these molecules might cross-link two ribopolymerases, giving rise to a precursor of the modern ribosome. A hybrid dimer, half polymerase and half proto-ribosome, could account for mRNA translocation before the advent of protein elongation factors.

scholarly journals Use of β3-methionine as an amino acid substrate of Escherichia coli methionyl-tRNA synthetase

2020 ◽  
Vol 209 (2) ◽  
pp. 107435 ◽  
Author(s):  
Giuliano Nigro ◽  
Sophie Bourcier ◽  
Christine Lazennec-Schurdevin ◽  
Emmanuelle Schmitt ◽  
Philippe Marlière ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Methionyl Trna Synthetase ◽  
Acid Substrate ◽  
Amino Acid Substrate

scholarly journals Amino Acid Toxicities of Escherichia coli That Are Prevented by Leucyl-tRNA Synthetase Amino Acid Editing

2007 ◽  
Vol 189 (23) ◽  
pp. 8765-8768 ◽  
Author(s):  
Vrajesh A. Karkhanis ◽  
Anjali P. Mascarenhas ◽  
Susan A. Martinis
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Editing

ABSTRACT Leucyl-tRNA synthetase (LeuRS) has evolved an editing function to clear misactivated amino acids. An Escherichia coli-based assay was established to identify amino acids that compromise the fidelity of LeuRS and translation. Multiple nonstandard as well as standard amino acids were toxic to the cell when LeuRS editing was inactivated.

Studies on Amino Acid Binding Proteins of Escherichia coli

1971 ◽  
Vol 69 (1) ◽  
pp. 243-245 ◽  
Author(s):  
Yasuhiro ANRAKU
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Binding Proteins ◽  
Amino Acid Binding
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