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Mutant strains of Tetrahymena thermophila defective in thymidine kinase activity: Biochemical and genetic characterization

Journal Article · · Mol. Cell. Biol.; (United States)
DOI:https://doi.org/10.1128/MCB.2.8.930· OSTI ID:5823334
;
Three mutant strains, one conditional, of Tetrahymena thermophila were defective in thymidine phosphorylating activity in vivo and in thymidine kinase activity in vitro. Nucleoside phosphotransferase activity in mutant cell extracts approached wild-type levels, suggesting that thymidine kinase is responsible for most, if not all, thymidine phosphorylation in vivo. Thymidine kinase activity in extracts of the conditional mutant strain was deficient when the cells were grown or assayed or both at the permissive temperature, implying a structural enzyme defect. Analysis of the reaction products from in vitro assays with partially purified enzymes showed that phosphorylation by thymidine kinase and nucleoside phosphotransferase occurred at the 5' position. Genetic analyses showed that the mutant phenotype was recessive and that mutations in each of the three mutant strains did not complement, suggesting allelism.
Research Organization:
Dept. of Biology, York Univ., Downsview, Ontario M3J 1P3
OSTI ID:
5823334
Journal Information:
Mol. Cell. Biol.; (United States), Journal Name: Mol. Cell. Biol.; (United States) Vol. 2:8; ISSN MCEBD
Country of Publication:
United States
Language:
English

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Related Subjects

550400* -- Genetics
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
AZINES
BIOCHEMICAL REACTION KINETICS
CHEMICAL REACTIONS
CILIATA
CONTROL
DEFECTS
ENZYME ACTIVITY
ENZYME INDUCTION
ENZYMES
GENE REGULATION
GENETIC CONTROL
GENOME MUTATIONS
HETEROCYCLIC COMPOUNDS
IN VITRO
IN VIVO
INVERTEBRATES
KINETICS
MICROORGANISMS
MUTANTS
MUTATIONS
NUCLEOSIDES
NUCLEOTIDES
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEST CONTROL
PHENOTYPE
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
PROTOZOA
PYRIMIDINES
REACTION KINETICS
RIBOSIDES
STRUCTURE-ACTIVITY RELATIONSHIPS
TETRAHYMENA
THYMIDINE
TRANSFERASES