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Two Poplar glycosyltransferase.Genes, PdGATL 1.1 and PdGATL1.2, Are Functional Orthologs to PARVUS/AtGATL 1 in Arabidopsis

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Molecular Plant 2009年第5期2卷 1040-1050页

作者： Yingzhen Kong Gongke Zhou Utku Avci Xiaogang Gu Chelsea Jones Yanbin Yin Ying Xu Michael G. Hahn Complex Carbohydrate Research Center The University of Georgia 315 Riverbend Road Athens GA 30602 USA BioEnergy Science Center The University of Georgia 315 Riverbend Road Athens GA 30602 USA Computational System Biology Lab Dept. of Biochemistry and Molecular Biology and Institute of Bioinformatics The University of Georgia Athens GA 30602 USA

Several genes in Arabidopsis, including PARVUS/AtGATL1, have been implicated in xylan synthesis. However, the biosynthesis of xylan in woody plants, where this polysaccharide is a major component of wood, is poorly understood. Here, we characterize two Populus genes, PdGATL 1.1 and PdGATL 1.2, the closest orthologs to the Arabidopsis PARVUS/GATL1 gene, with respect to their gene expression in poplar, their sub-cellular localization, and their ability to complement the parvus mutation in Arabidopsis. Overexpression of the two poplar genes in the parvus mutant rescued most of the defects caused by the parvus mutation, including morphological changes, collapsed xylem, and altered cell wall monosaccharide composition. Quantitative RT-PCR showed that PdGATL1.1 is expressed most strongly in developing xylem of poplar. In contrast, PdGATL1.2 is expressed much more uniformly in leaf, shoot tip, cortex, phloem, and xylem, and the transcript level of PdGATL1.2 is much lower than that of PdGATL 1.1 in all tissues examined. Sub-cellular localization experiments showed that these two proteins are localized to both ER and Golgi in comparison with marker proteins resident to these sub-cellular compartments. Our data indicate that PdGATLI.1 and PdGATL1.2 are functional orthologs of PARVUS/ GATL1 and can play a role in xylan synthesis, but may also have role（s） in the synthesis of other wall polymers.

关键词： Arabidopsis thaliana poplar xylan glycosyltransferase.

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Sub-Compartmental Organization of Golgi-Resident N-Glycan Processing Enzymes in Plants

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Molecular Plant 2011年第2期4卷 220-228页

作者： Jennifer Schoberer Richard Strasser School of Life Sciences Oxford Brookes University Headington Campus Gipsy Lane Oxford OX3 OBP UK Department of Applied Genetics and Cell Biology University of Natural Resources and Life Sciences Vienna Austria

In all eukaryotes, the Golgi apparatus is the main site of protein glycosylation. It is widely accepted that the glycosidases and glycosyltransferase. involved in N-glycan processing are found concentrated within the Golgi stack where they provide their function. This means that enzymes catalyzing early steps in the processing pathway are located mainly at the cis-side, whereas late-acting enzymes mostly locate to the trans-side of the stacks, creating a non-uniform distribution along the cis-trans axis of the Golgi. There is compelling evidence that the information for their sorting to specific Golgi cisternae depends on signals encoded in the proteins themselves as well as on the trafficking machinery that recognizes these signals and it is believed that cisternal sub-compartmentalization is achieved and maintained by a combination of retention and retrieval mechanisms. Yet, the signals, mechanism（s）, and molecular factors involved are still unknown. Here, we address recent findings and summarize the current understanding of this fundamental process in plant cell biology.

关键词： Endomembrane system Golgi apparatus glycosylation glycosyltransferase.

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