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

1 Citation (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

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S-Adenosylmethionine
Tobacco
Methyltransferases
Transferases
Topology
Membranes
Proteins
Golgi Apparatus
Digestion
Catalytic Domain
Peptide Hydrolases
Fluorescence
Amino Acids
Substrates

All Science Journal Classification (ASJC) codes

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

Cite this

Membrane topology of Golgi-localized probable S-adenosylmethioninedependent methyltransferase in tobacco (Nicotiana tabacum) BY-2 cells. / Liu, Jianping; Hayashi, Kyoko; Matsuoka, Ken.

In: Bioscience, Biotechnology and Biochemistry, Vol. 79, No. 12, 01.01.2015, p. 2007-2013.

Research output: Contribution to journalArticle

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