| First Author | Perryman SM | Year | 1986 |
| Journal | Mol Biol Evol | Volume | 3 |
| Issue | 4 | Pages | 313-21 |
| PubMed ID | 3444407 | Mgi Jnum | J:32376 |
| Mgi Id | MGI:79875 | Doi | 10.1093/oxfordjournals.molbev.a040400 |
| Citation | Perryman SM, et al. (1986) Sequence of a cDNA for mouse thymidylate synthase reveals striking similarity with the prokaryotic enzyme. Mol Biol Evol 3(4):313-21 |
| abstractText | We report the nucleotide sequence of a cloned cDNA, pMTS-3, that contains a 1-kb insert corresponding to mouse thymidylate synthase (E.C. 2.1.1.45). The open reading frame of 921 nucleotides from the first AUG to the termination codon specifies a protein with a molecular mass of 34,962 daltons. The predicted amino acid sequence is 90% identical with that of the human enzyme. The mouse sequence also has an extremely high degree of similarity (as much as 55% identity) with prokaryotic thymidylate synthase sequences, indicating that thymidylate synthase is among the most highly conserved proteins studied to date. The similarity is especially pronounced (as much as 80% identity) in the 44-amino-acid region encompassing the binding site for deoxyuridylic acid. The cDNA sequence also suggests that mouse thymidylate synthase mRNA lacks a 3' untranslated region, since the termination codon, UAA, is followed immediately by a poly(A) segment. |
