Partial purification and characterization of the specific protein-lysine N-methyltransferase of YL32, a yeast ribosomal protein.

Lobet, Y.;Colson, Charles;Lhoest, J.
(1989) Biochimica et Biophysica Acta : international journal of biochemistry and biophysics — Vol. 997, n° 3, p. 224-231 (1989)

Files

No attached file found for this publication.

Details

Authors
  • Lobet, Y.
    Author
  • Colson, CharlesUCLouvain
    Author
  • Lhoest, J.
    Author
Abstract
YL23 and YL32 are two of the three most heavily methylated ribosomal proteins of Saccharomyces cerevisiae. Using an in vitro assay, it was determined that they are methylated by two distinct enzymes. The protein-lysine N-methyltransferase that methylates YL32 was partially purified by affinity and ion-exchange chromatography. Its molecular mass was estimated to be 82 kDa, and its isoelectric point to be 4.45. Optimum activity was expressed at pH 7.5, and the enzyme was irreversibly inactivated at pH lower than 5.0. The Km of the enzyme for AdoMet is 1.7 +/- 0.4 microM, and the Ki toward AdoHcy was 0.71 microM. Formation of epsilon-N-dimethyllysine was observed to occur in two steps via epsilon-N-monomethyllysine. Like other protein-lysine N-methyltransferases, the methylase of YL32 exhibits a high substrate specificity.
Affiliations

Citations

  • APA
  • Chicago
  • FWB

Lobet, Y., Colson, C., & Lhoest, J. (1989). Partial purification and characterization of the specific protein-lysine N-methyltransferase of YL32, a yeast ribosomal protein. Biochimica et Biophysica Acta : international journal of biochemistry and biophysics, 997(3), 224-231. https://doi.org/10.1016/0167-4838(89)90191-X (Original work published 1989)