High impact information on Och

• We conclude from these properties that this mutant cell line contains an ochre nonsense mutation (UAA) in the structural gene for HGPRT [1].
• Within a 67-base-pair exon of the rd PDE beta-subunit gene, we identified a nonsense ochre mutation (a C----A transversion in codon 347) that truncates the normal gene product, eliminating more than one-half of the peptide chain, including the putative catalytic domain [2].
• Multicopy tRNA expression plasmids were directly injected into skeletal muscle and into the hearts of transgenic mice carrying a reporter gene with an ochre mutation [3].
• The product of suppression (chloramphenicol acetyltransferase) accumulates linearly with increases in suppressor tRNA concentration to the point where the ochre-suppressing tRNA(Ser) is in four- to fivefold excess over the endogenous tRNA(Ser) [3].
• Double-site immunoassay and P. falciparum transient transfection using the reporter luciferase gene demonstrated translation through the internal ochre codon [4].

Biological context of Och

• Nucleotide sequence and evolution of the rat mitochondrial cytochrome b gene containing the ochre termination codon [5].
• We evaluated both the in vitro and in vivo efficiencies of readthrough of ochre codons in 2 genes with the tRNA suppressor gene [6].

Anatomical context of Och

• The wild-type amber (UAG) and in vitro-generated ochre (UAA) readthrough codon derivatives replicated in protoplasts [7].
• The scFv gene in one of these clones was reamplified to introduce the ochre codons, and then expressed in the bacterial periplasm as the soluble antibody fragment [8].

Associations of Och with chemical compounds

• On account of the spontaneous oxidation process, the colour of PPD increases and becomes ochre-brown in a few days, showing an absorption peak at lambda = 510 nm with shoulder at about 440 to 460 nm [9].

References