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Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.
From the results, methionine excision catalyzed by MAP is shown to obey the following rule: the catalytic efficiency of MAP, and therefore the extent of cleavage, decreases in parallel with the increasing of the maximal side-chain length of the amino acid in the penultimate position. Expand
Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction.
Sets of parameters governing the rules were determined under various mutagenic conditions including the addition of MnCl2 and validity of the rules was assessed in several mutagenesis experiments showing that a wide range of substitution frequencies including AT-->GC and GC-->AT transitions as well as AT-->TA transversions can be obtained at will. Expand
Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl‐tRNA hydrolase
The structure of crystalline peptidyl‐tRNA hydrolase could be solved at 1.2 Å resolution and indicates a single α/β globular domain built around a twisted mixed β‐sheet, similar to the central core of an aminopeptidase from Aeromonas proteolytica. Expand
Structural basis for tRNA-dependent amidotransferase function.
Comparison of GatD and L-asparaginase structures shows how the motion of a beta hairpin region containing a crucial catalytic threonine may control the overall reaction cycle of GatDE. Expand
Sequence of a 1.26‐kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon.
The nucleotide sequence of a 1.26‐kb pair DNA fragment containing the structural gene for Escherichia coli initiation factor IF3 has been determined and the presence of AUU as the translational initiator codon is determined. Expand
Structural Basis of RNA-Dependent Recruitment of Glutamine to the Genetic Code
Glutaminyl–transfer RNA (Gln-tRNAGln) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNAGln by the heterodimeric Glu-tRNAGln amidotransferase GatDE. Here we report theExpand
Role of d-Cysteine Desulfhydrase in the Adaptation of Escherichia coli to d-Cysteine*
In agreement with a role of the desulfhydrase in sulfur metabolism, yedO expression was induced under conditions of sulfate limitation and growth protection against d-cysteine in minimal medium was conferred by the simultaneous addition of isoleucines, leucine, and valine. Expand
Pyrophosphatase is essential for growth of Escherichia coli.
The ppa gene for inorganic pyrophosphatase is essential for the growth of Escherichia coli. A recombinant with a chromosomal ppa::Kanr lesion and a temperature-sensitive replicon with a ppa+ geneExpand
Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli.
In bacteria, as well as in chloroplasts and mitochondria, the free amino group of the methionylated initiator tRNA(fMet) is specifically modified by the addition of a formyl group. The importance ofExpand
Metabolism of d-Aminoacyl-tRNAs inEscherichia coli and Saccharomyces cerevisiae Cells*
The results indicate that an unexpected high number of d-amino acids can impair the bacterium growth through the accumulation ofd-Aminoacyl-tRNA molecules and that d-Tyr-tRNATyr deacylase has a specificity broad enough to recycle any of these molecules. Expand