Differential effects of human and plant N-acetylglucosaminyltransferase I (GnTI) in plants

M.G.L. Henquet, B. Heinhuis, J.W. Borst, J. Eigenhuijsen, M. Schreuder, D. Bosch, A.R. van der Krol

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)

Abstract

In plants and animals, the first step in complex type N-glycan formation on glycoproteins is catalyzed by N-acetylglucosaminyltransferase I (GnTI). We show that the cgl1-1 mutant of Arabidopsis, which lacks GnTI activity, is fully complemented by YFP-labeled plant AtGnTI, but only partially complemented by YFP-labeled human HuGnTI and that this is due to post-transcriptional events. In contrast to AtGnTI-YFP, only low levels of HuGnTI-YFP protein was detected in transgenic plants. In protoplast co-transfection experiments all GnTI-YFP fusion proteins co-localized with a Golgi marker protein, but only limited co-localization of AtGnTI and HuGnTI in the same plant protoplast. The partial alternative targeting of HuGnTI in plant protoplasts was alleviated by exchanging the membrane-anchor domain with that of AtGnTI, but in stably transformed cgl1-1 plants this chimeric GnTI still did not lead to full complementation of the cgl1-1 phenotype. Combined, the results indicate that activity of HuGnTI in plants is limited by a combination of reduced protein stability, alternative protein targeting and possibly to some extend to lower enzymatic performance of the catalytic domain in the plant biochemical environment
Original languageEnglish
Pages (from-to)535-547
JournalTransgenic Research
Volume19
Issue number4
DOIs
Publication statusPublished - 2010

Keywords

  • arabidopsis-thaliana
  • molecular-cloning
  • linked glycans
  • expression
  • golgi
  • transmembrane
  • mutant
  • beta-1,2-n-acetylglucosaminyltransferase-i
  • transformation
  • transferase

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