The Golgi localization of Arabidopsis thaliana β1,2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences

The Golgi localization of Arabidopsis thaliana β1,2-xylosyltransferase in plant cells is... To investigate the targeting of proteins to the plant Golgi we studied Arabidopsis thaliana β1,2-xylosyltransferase (XylT), a glycosyltransferase which is unique to plants and some invertebrates. Different deletion constructs of the putative cytoplasmic (C)-transmembrane (T)-stem (S) region of the enzyme were transiently expressed in the tobacco-related model plant species Nicotiana benthamiana. Subcellular localization of fusion proteins between CTS, CT, T, or C domains and the reporter molecule green fluorescent protein by fluorescence microcopy and density-gradient centrifugation revealed that the CT region alone is sufficient to sustain Golgi retention of XylT without the contribution of any luminal sequences. The finding of an incomplete retention by the T region alone suggests an important auxiliary role of the C domain in Golgi retention of the protein. However, the C segment did not confer any Golgi retention by itself, as the respective fusion protein was found exclusively in the cytoplasm. These results provide evidence that plant and mammalian cells rely on similar mechanisms to deliver glycosyltransferases to the Golgi apparatus. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

The Golgi localization of Arabidopsis thaliana β1,2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 2002 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1016061815748
Publisher site
See Article on Publisher Site

Abstract

To investigate the targeting of proteins to the plant Golgi we studied Arabidopsis thaliana β1,2-xylosyltransferase (XylT), a glycosyltransferase which is unique to plants and some invertebrates. Different deletion constructs of the putative cytoplasmic (C)-transmembrane (T)-stem (S) region of the enzyme were transiently expressed in the tobacco-related model plant species Nicotiana benthamiana. Subcellular localization of fusion proteins between CTS, CT, T, or C domains and the reporter molecule green fluorescent protein by fluorescence microcopy and density-gradient centrifugation revealed that the CT region alone is sufficient to sustain Golgi retention of XylT without the contribution of any luminal sequences. The finding of an incomplete retention by the T region alone suggests an important auxiliary role of the C domain in Golgi retention of the protein. However, the C segment did not confer any Golgi retention by itself, as the respective fusion protein was found exclusively in the cytoplasm. These results provide evidence that plant and mammalian cells rely on similar mechanisms to deliver glycosyltransferases to the Golgi apparatus.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 13, 2004

References

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