The elaborate route for UDP-arabinose delivery into the Golgi of plants
[3];
[1];
- School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia,, Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702,
- Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702,
- Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602,
- School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia,
- Centro de Biotecnología Vegetal, Fondo de Areas Prioritarias Center for Genome Regulation, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Santiago RM 8370146, Chile,
- Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702,, Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720
In plants, L-Arabinose (Ara) is a key component of cell wall polymers, glycoproteins, as well as flavonoids, and signaling peptides. Whereas the majority of Ara found in plant glycans occurs as a furanose ring (Araf), the activated precursor has a pyranose ring configuration (UDP-Arap). The biosynthesis of UDP-Arap mainly occurs via the epimerization of UDP-xylose (UDP-Xyl) in the Golgi lumen. Given that the predominant Ara form found in plants is Araf, UDP-Arap must exit the Golgi to be interconverted into UDPAraf by UDP-Ara mutases that are located outside on the cytosolic surface of the Golgi. Subsequently, UDP-Araf must be transported back into the lumen. During this step it is vital because glycosyltransferases, the enzymes mediating the glycosylation reactions, are located within the Golgi lumen, and UDP-Arap, synthesized within the Golgi, is not their preferred substrate. Therefore, the transport of UDP-Araf into the Golgi is a prerequisite. Although this step is critical for cell wall biosynthesis and the glycosylation of proteins and signaling peptides, the identification of these transporters has remained elusive. In this study, we present data demonstrating the identification and characterization of a family of Golgilocalized UDP-Araf transporters in Arabidopsis. The application of a proteoliposome-based transport assay revealed that four members of the nucleotide sugar transporter (NST) family can efficiently transport UDP-Araf in vitro. Subsequent analysis of mutant lines affected in the function of these NSTs confirmed their role as UDP-Araf transporters in vivo.
- Research Organization:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- Grant/Contract Number:
- AC02-05CH11231
- OSTI ID:
- 1579294
- Alternate ID(s):
- OSTI ID: 1393224
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Vol. 114 Journal Issue: 16; ISSN 0027-8424
- Publisher:
- Proceedings of the National Academy of SciencesCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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