PMID: 2504290Aug 31, 1989Paper

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

Biochimica Et Biophysica Acta
Y LobetC Colson

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.

References

Feb 1, 1976·Archives of Biochemistry and Biophysics·F N ChangB M Dancis
Nov 1, 1971·Analytical Biochemistry·L L Houston
Sep 11, 1984·Nucleic Acids Research·R J LeerR J Planta
Jun 15, 1984·European Journal of Biochemistry·J LhoestC Colson

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Citations

May 2, 2002·Proceedings of the National Academy of Sciences of the United States of America·Sang-Won LeeRichard D Smith
Jul 6, 2007·Molecular Microbiology·Bogdan Polevoda, Fred Sherman
Feb 25, 2014·Biochimica Et Biophysica Acta·Kaitlyn E Moore, Or Gozani
Oct 24, 2017·Nature Cell Biology·Michael A ReidJason W Locasale
Aug 13, 2005·The Journal of Biological Chemistry·Tanya R Porras-YakushiSteven Clarke
Sep 29, 2006·The Journal of Biological Chemistry·Tanya R Porras-YakushiSteven Clarke
Jan 1, 1997·Microbiology and Immunology·S Y SeongW H Chang
Apr 5, 2000·The Journal of Biological Chemistry·A BecchettiD C Eaton
Jul 27, 2000·American Journal of Physiology. Cell Physiology·N F Al-BaldawiD C Eaton

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