URA3 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome V.
Dietrich FS, Mulligan J, Hennessy K, Yelton MA, Allen E, Araujo R, Aviles E, Berno A, Brennan T, Carpenter J, Chen E, Cherry JM, Chung E, Duncan M, Guzman E, Hartzell G, Hunicke-Smith S, Hyman RW, Kayser A, Komp C, Lashkari D, Lew H, Lin D, Mosedale D, Davis RW
Nature387(6632 Suppl)78-81(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

we showed that high levels of copper (previously shown to elevate CUP1 transcription) lead to a substantial elevation in rate of both interhomolog and intra/sister chromatid recombination in the CUP1 array; recombination events that delete the URA3 insertion from the CUP1 array occur at a rate of >10(-3)/division in unselected cells.
Title: Properties of Mitotic and Meiotic Recombination in the Tandemly-Repeated

We found that mutations were scattered throughout the open reading frame of the URA3 gene but clustered to several hotspots with base substitutions/deletions at homo-polymeric runs. Surprisingly, we only detected two multiple mutants out of over 300 sequenced mutation events.
Title: Microhomology-mediated end joining induces hypermutagenesis at breakpoint junctions.

Analysis of a triple mutant cube shows small interactions between phosphodianion gripper side chains, which are consistent with steric crowding of the side chains around the phosphodianion at wild-type OMPDC
Title: Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.

investigation of OMPDC/URA3 biocatalysis: substrate specificity; kinetics; conformational changes during substrate binding/decarboxylation
Title: Catalysis by orotidine 5'-monophosphate decarboxylase: effect of 5-fluoro and 4'-substituents on the decarboxylation of two-part substrates.

Greater enthalpic transition state stabilization available from more extensive loop-substrate interactions for the S. cerevisiae-catalyzed reaction is largely balanced by a larger entropic requirement for immobilization of the larger loop at this enzyme.
Title: An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organisms.