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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
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
Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase.
The 3-D structure of the peptidyl-tRNA hydrolase from the archaea Sulfolobus solfataricus has been solved and the crystalline structure of this enzyme indicates the formation of a dimer, which clearly distinguish the active site of the archaeal/eucaryal hydrolases from that of the bacterial/eUCaryal ones. Expand
Peptidyl-tRNA hydrolase from Sulfolobus solfataricus.
Evidence is presented that YHR189w, the gene encoding a bacterial-like PTH, should be involved in mitochondrial function, and the occurrence in many eukaryotes of two distinct PTH activities, either of a bacterial or of an archaeal type is suggested. Expand
Yeast diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase behaves as a dinucleoside tetraphosphate synthetase.
The diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase, recently observed in yeast, is shown to be capable of catalyzing the synthesis of Ap4A from ATP + ADP, i.e., the reverse reaction of the phosphorolysis ofAp4A. Expand
Catabolism of bis(5'-nucleosidyl) tetraphosphates in Saccharomyces cerevisiae.
Disruption of APA2 and/or APA1 shows that none of these genes is essential for the viability of Saccharomyces cerevisiae, and supports the conclusion that, in vivo, Ap4A phosphorylase I, participates in the catabolism rather than the synthesis of the bis(5'-nucleosidyl) tetraphosphates. Expand
Receptor site for the 5'-phosphate of elongator tRNAs governs substrate selection by peptidyl-tRNA hydrolase.
It is proposed that the capacity of the 5'-phosphate of a tRNA to reach or not a receptor site is the main identity element governing generic selection of elongator tRNAs. Expand
NMR-based substrate analog docking to Escherichia coli peptidyl-tRNA hydrolase.
Functional value is given to this model by showing that the enzyme becomes confusable with an aminoacyl-tRNA hydrolase upon mutagenesis of Asn10 and reinterpreting already obtained site-directed mutagesis data. Expand
RNA-binding Site of Escherichia coli Peptidyl-tRNA Hydrolase
The RNA-binding site of Escherichia coli peptidyl-tRNA hydrolase is characterized and NMR mapping indicates amino acid residues sensitive to RNA binding in the following: the enzyme active site region; the helix-loop covering the active site; and the region including Leu-95 and the bordering residues 111–117, supposed to form the boundary between the tRNA core and the peptidol-CCA moiety-binding sites. Expand