EC Number   |
Protein Variants |
Reference |
|---|
   3.6.1.74 | E345A |
site-directed mutagenesis, the mutant cannot complement Saccharomyces cerevisiae CEG1 deficient mutants |
762029 |
| 3.6.1.74 | K192N |
site-directed mutagenesis, the mutation in the nucleotide-binding site completely abolishes RNA triphosphatase and nucleoside triphosphatase activities of Semliki Forest virus Nsp2 and Nsp2-N (N-terminal fragment) |
761423 |
| 3.6.1.74 | K294A |
site-directed mutagenesis, the mutant cannot complement Saccharomyces cerevisiae CEG1 deficient mutants |
762029 |
| 3.6.1.74 | K458A |
site-directed mutagenesis, the mutant cannot complement Saccharomyces cerevisiae CEG1 deficient mutants |
762029 |
| 3.6.1.74 | K460A |
site-directed mutagenesis, the mutant cannot complement Saccharomyces cerevisiae CEG1 deficient mutants |
762029 |
| 3.6.1.74 | more |
CaCET1 rescues CET1-deficient Saccharomyces cerevisiae cells when expressed under the control of the ADH1 promoter, whereas the human capping enzyme derivatives that are active for TPase activity but defective in mRNA 5'-guanylyltransferase (GTase) activity do not. Yeast two-hybrid analysis reveals that Candida albicans Cet1p can bind to the Saccharomyces cerevisiae GTase in addition to its endogenous partner, the Candida albicans GTase. In contrast, neither the full-length human capping enzyme nor its TPase domain interact with the yeast GTase. The failure of the human TPase activity to complement an Saccharomyces cerevisiae cet1DELTA null mutation is attributable, at least in part, to the inability of the human capping enzyme to associate with the yeast GTase, and the physical association of GTase and TPase is essential for the function of the capping enzyme in vivo. Complementation of an Saccharomyces cerevisiae ceg1DELTA null mutation by Candida albicans CET1 and interaction of CaCet1p with ScCeg1p (alpha-subunit with mRNA 5'-guanylyltransferase (GTase) activity) |
-, 761075 |
| 3.6.1.74 | more |
construction of C-terminal deletion and of N-terminal mutants (His-CAP1a (1-213) and His-CAP1a (229-597)) of hCAP1a |
760471 |
| 3.6.1.74 | more |
construction of His-tagged C- and N-terminal deletion mutants, His-Cet1(1-265) and His-Cet1(205-549), respectively, and expression in Escherichia coli |
-, 760470 |
| 3.6.1.74 | more |
generation of ceg1-25 mutation of the yeast mRNA guanylyltransferase (capping enzyme) causing a temperature-sensitive growth defect. Construction of truncated mutant Cet1 proteins, Cet1(201-549) and Cet1(246-549). Mutant Cet1(201-549) has RNA triphosphatase activity, heterodimerizes with and stimulates Ceg1 in vitro, and suffices when expressed in single copy for cell growth in vivo, but the more extensively truncated mutant Cet1(246-549) fails to stimulate Ceg1 in vitro and is lethal when expressed in single copy in vivo, while it also has RNA triphosphatase activity. Construction and complementation of a DELTAcet1 mutant by mouse capping enzyme, overview |
-, 761894 |
| 3.6.1.74 | R299A |
site-directed mutagenesis, the mutant cannot complement Saccharomyces cerevisiae CEG1 deficient mutants |
762029 |
