• Publications
  • Influence
Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution.
The crystal structure of RNase H from Escherichia coli has been determined by the multiple isomorphous replacement method, and refined by the stereochemically restrained least-squares procedure to a crystallographic R-factor of 0.196 at 1.48 A resolution, and reveals the details of hydrogen bonding, electrostatic and hydrophobic interactions between intra- and intermolecular residues.
Essential structure of E. coli promoter: effect of spacer length between the two consensus sequences on promoter function.
A promoter with the consensus sequence(TTGACA and TATAAT) at -35 and -10 regions was constructed, and the distance between the two consensus sequences was independently altered at two restriction
Three-dimensional structure of ribonuclease H from E. coli
THE three-dimensional structure of RNase H from Escherichia coli was determined at 1.8 Å resolution by X-ray crystallography. The enzyme was found to belong to the α + β class of structures,
An alternative approach to deoxyoligonucleotides as hybridization probes by insertion of deoxyinosine at ambiguous codon positions.
Oligonucleotide probes with deoxyinosine residues at ambiguous points seem to be useful as hybridization probes for cloning genes for proteins containing amino acids with degenerate codons.
NMR studies of a DNA containing 8-hydroxydeoxyguanosine.
NMR data indicate that the 8-hydroxyguanine (oh8G) base takes a 6,8-diketo tautomeric form and is base-paired to C with Watson-Crick type hydrogen bonds in a B-form structure.
Identification of the amino acid residues involved in an active site of Escherichia coli ribonuclease H by site-directed mutagenesis.
Determination of the kinetic parameters for the mutated enzymes using the chemically synthesized nonanucleotide duplex as a substrate demonstrated that these residues are involved in the catalytic site rather than the substrate-binding site, which strongly suggests that they are also involvement in the active site of these RTs and RT related enzymes.
X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer.
The x-ray structure of T4 endonuclease V, an enzyme responsible for the first step of a pyrimidine-dimer-specific excision-repair pathway, was determined at a 1.6-angstrom resolution and suggests the residues involved in the substrate binding and the catalysis of the glycosylation reaction.
Secretion in yeast of human lysozymes with different specific activities created by replacing valine-110 with proline by site-directed mutagenesis.
The results suggest that cis/trans isomerization of prolyl peptide bonds probably occurs in vivo and that the conformational change of protein as well as point mutations in genes might influence the molecular evolution of the protein.
Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins.
The sequence provides direct evidence that diphthamide (2-carboxy-amido-3-(trimethylammonio)propyl]histidine), the site of ADP-ribosylation by diphtheria toxin, is produced by post-translational modification of a histidine residue in the primary translational product.
Molecular cloning of the human cholecystokinin gene by use of a synthetic probe containing deoxyinosine.
CCK appears to be encoded by a single-copy gene in the haploid human genome, as revealed by genomic Southern hybridization analysis, suggesting that the same gene is expressed both in gut and brain.