Thymidylate Synthase Heterogeneity Assessed by Monoclonal Antibodies

@inproceedings{Goos2002ThymidylateSH,
  title={Thymidylate Synthase Heterogeneity Assessed by Monoclonal Antibodies},
  author={B Gołos and Elżbieta Wałajtys-Rode and Anna Porębska and Joanna Cieśla and M Dabrowska and Zbigniew Zieliński and Wojciech Rode},
  year={2002}
}
Thymidylate synthase (TS; EC 2.1.1.45) catalyzes N5,10-methylenetetrahydrofolate-dependent methylation of dUMP. Purified preparations of the enzyme from regenerating rat liver, L1210 cell and Trichinella spiralis muscle larvae, and recombinant rat hepatoma and mouse L1210 thymidylate synthases, analyzed with the use of SDS Polyacrylamide gel electrophoresis, show heterogeneity, reflected by an additional distinct band (Figure 1; cf. ref. 1), located too close to the main band to enable… Expand
The effect of Arg209 to Lys mutation in mouse thymidylate synthase.
TLDR
It is documented that mouse thymidylate synthase R209, similar to the corresponding L. casei R218, is essential for both dUMP binding and enzyme reaction. Expand
Altered mouse leukemia L1210 thymidylate synthase, associated with cell resistance to 5-fluoro-dUrd, is not mutated but rather reflects posttranslational modification.
TLDR
Direct sequencing of products obtained from RT-PCR proved both nucleotide sequences to be identical to the mouse thymidylate synthase coding sequence published earlier, suggesting that the altered properties of TSr are caused by a factor different than protein mutation, presumably posttranslational modification. Expand
Binding and repression of translation of the cognate mRNA by Trichinella spiralis thymidylate synthase differ from the corresponding interactions of the human enzyme.
TLDR
It is shown that mRNA binding requires a methionine or an adduct at the N-terminus of TS, but that the translational repression effect does not, and that chicken liver dihydrofolate reductase, which is incapable of binding to T. spiralis TS mRNA, repressed the translation of TS. Expand
Developmental arrest in Caenorhabditis elegans dauer larvae causes high expression of enzymes involved in thymidylate biosynthesis, similar to that found in Trichinella muscle larvae
TLDR
High thymidylate synthase expression in developmentally arrested larvae, demonstrated also at the mRNA and protein levels, is in agreement with a global cell cycle arrest of dauer larvae and indicates this unusual cell cycle regulation pattern can be shared by developmentally arrests larvae of C. elegans and the two Trichnella species. Expand

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TLDR
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TLDR
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TLDR
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