Related (α)N- and (ε)N-methyltransferases methylate the large and small subunits of Rubisco

Z. Ying, R. M. Mulligan, N. Janney, M. Royer, R. L. Houtz

Research output: Contribution to journalArticlepeer-review


Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is methylated at the α amino position of the N-terminal methionyl residue of the processed and assembled form of the small subunit (SS), and is also methylated in some species at the ε-amino group of lysine- 14 in the large subunit (LS). The gene (rbcMTS) and cDNAs for the SS (α)N-methyltransferase (SSMT) from spinach (Spinach oleracea) have been cloned, sequenced, and expressed. The gene is closely related to a previously characterized LS methyltransferase (Rubisco LSMT) cDNA from pea (Rubisco LSMT) and a Rubisco LSMT gene from tobacco. Sequence analysis of the cDNA and transcript mapping experiments demonstrate that the rbcMT-S pre-mRNAs experience alternative 3' splice site selection, such that mRNAs for a long form with a four amino acid insertion and a short form are expressed at approximately equal abundance. The coding sequence of spinach SSMT includes a putative targeting presequence with sequence identity at a plastid processing site. A N-terminal truncated form of spinach SSMT was expressed and purified from E. coli cells. Both long and short forms of the cDNAs were shown to catalyze methylation of the a amine of the N-terminal methionine of the SS of Rubisco.

Original languageEnglish
Pages (from-to)173-184
Number of pages12
JournalActa Biologica Hungarica
Issue number2-4
StatePublished - 1998


  • N-methylmethionine
  • N-methyltransferases
  • Protein methylation
  • Rubisco
  • Trimethyllysine

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology
  • General Environmental Science
  • Neurology


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