Membrane topology of Golgi-localized probable S-adenosylmethioninedependent methyltransferase in tobacco (Nicotiana tabacum) BY-2 cells

Jianping Liu, Kyoko Hayashi, Ken Matsuoka

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

S-adenosylmethionine (SAM)-dependent methyltransferases (MTases) transfer methyl groups to substrates. In this study, a novel putative tobacco SAM-MTase termed Golgi-localized methyl transferase 1 (GLMT1) has been characterized. GLMT1 is comprised of 611 amino acids with short N-terminal region, putative transmembrane region, and C-terminal SAM-MTase domain. Expression of monomeric red fluorescence protein (mRFP)-tagged protein in tobacco BY-2 cell indicated that GLMT1 is a Golgi-localized protein. Analysis of the membrane topology by protease digestion suggested that both C-terminal catalytic region and N-terminal region seem to be located to the cytosolic side of the Golgi apparatus. Therefore, GLMT1 might have a different function than the previously studied SAM-MTases in plants.

Original languageEnglish
Pages (from-to)2007-2013
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Volume79
Issue number12
DOIs
Publication statusPublished - Jan 1 2015

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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