Identification of a novel Golgi-localized putative glycosyltransferase protein in Arabidopsis thaliana

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  • Rzepecka Natalia
    Graduate School of Humanities and Sciences, Ochanomizu University
  • Ito Yoko
    Institute for Human Life Science, Ochanomizu University
  • Yura Kei
    Graduate School of Humanities and Sciences, Ochanomizu University Institute for Human Life Science, Ochanomizu University Natural Science Division, Faculty of Core Research, Ochanomizu University Graduate School of Advanced Science and Engineering, Waseda University
  • Ito Emi
    Institute for Human Life Science, Ochanomizu University Institute for Women’s Education in Science, Technology, Engineering, Arts and Mathematics, Ochanomizu University
  • Uemura Tomohiro
    Graduate School of Humanities and Sciences, Ochanomizu University Institute for Human Life Science, Ochanomizu University Natural Science Division, Faculty of Core Research, Ochanomizu University Institute for Women’s Education in Science, Technology, Engineering, Arts and Mathematics, Ochanomizu University

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  • Identification of a novel Golgi-localized putative glycosyltransferase protein in <i>Arabidopsis thaliana</i>

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<p>SNAREs play an important role in the process of membrane trafficking. In the present research, we investigated subcellular localization of an uncharacterized Arabidopsis thaliana protein reported to interact with a trans-Golgi network-localized Qa-SNARE, SYNTAXIN OF PLANTS 43. Based on the similarity of its amino acid sequence to metazoan fucosyltransferases, we have named this novel protein AtGTLP (Arabidopsis thaliana GlycosylTransferase-Like Protein) and predicted that it should be a member of yet uncharacterized family of Arabidopsis fucosyltransferases, as it shows no significant sequence similarity to fucosyltransferases previously identified in Arabidopsis. AtGTLP is a membrane-anchored protein, which exhibits a type II-like topology, with a single transmembrane helix and a globular domain in the C-terminal part of its amino acid sequence. Colocalization data we collected suggest that AtGTLP should localize mainly to Golgi apparatus, especially to certain zones of trans-Golgi. As single atgtlp−/− mutants showed no obvious difference in phenotype (primary root length and fresh mass), AtGTLP and proteins related to AtGTLP with high similarity in amino acid sequences may have redundant functions.</p>

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