Source:http://linkedlifedata.com/resource/pubmed/id/15840645
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2005-7-4
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pubmed:abstractText |
AtAGP17, AtAGP18 and AtAGP19 are homologous genes encoding three putative glycosylphosphatidylinositol (GPI)-anchored classical arabinogalactan-proteins (AGPs) in Arabidopsis. They are distinguished from other AGPs by a short, C-terminal lysine-rich region. Organ-specific expression of these genes was revealed by Northern blot analysis. AtAGP17 was strongly expressed in leaves and stems, and weakly expressed in flowers and roots; AtAGP18 was strongly expressed in flowers, and moderately expressed in roots, stems and young leaves; and AtAGP19 was strongly expressed in stems, moderately expressed in flowers and roots, and weakly expressed in young leaves. One of these genes, AtAGP17, was expressed and purified as a green fluorescent protein (GFP) fusion protein in transgenic tobacco cells using hydrophobic interaction chromatography, size exclusion chromatography and reverse phase high-performance liquid chromatography. The fusion (glyco)protein produced a characteristic AGP 'smear' with a molecular mass of 80-150 kDa when detected by Western blot analysis. Glycosyl composition and linkage analyses of purified GFP-AtAGP17 showed that carbohydrate accounted for approximately 86% of the molecule, with arabinose and galactose as major, and rhamnose and glucuronic acid as minor glycosyl residues and with 1,3,6-galactose, 1,4-glucuronic acid, 1,3-galactose and terminal arabinose as major linkages. GFP-AtAGP17 was also precipitated by beta-Yariv reagent, further confirming that AtAGP17 is a bona fide AGP. Confocal fluorescence microscopy of plasmolysed, transformed cells indicated that AtAGP17 is localized on the plasma membrane and in Hechtian strands. Hydroxyproline (Hyp) glycoside profiles of GFP-AtAGP17 in conjunction with the deduced protein sequence also served to corroborate the Hyp contiguity hypothesis, which predicts contiguous Hyp residues as attachment sites for arabinosides and clustered, non-contiguous Hyp residues as attachment sites for arabinogalactan polysaccharides.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyproline,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Mucoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/arabinogalactan proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0032-0781
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
975-84
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15840645-Amino Acid Sequence,
pubmed-meshheading:15840645-Arabidopsis,
pubmed-meshheading:15840645-Arabidopsis Proteins,
pubmed-meshheading:15840645-Base Sequence,
pubmed-meshheading:15840645-DNA, Plant,
pubmed-meshheading:15840645-Gene Expression,
pubmed-meshheading:15840645-Genes, Plant,
pubmed-meshheading:15840645-Hydroxyproline,
pubmed-meshheading:15840645-Lysine,
pubmed-meshheading:15840645-Molecular Sequence Data,
pubmed-meshheading:15840645-Molecular Structure,
pubmed-meshheading:15840645-Molecular Weight,
pubmed-meshheading:15840645-Mucoproteins,
pubmed-meshheading:15840645-Multigene Family,
pubmed-meshheading:15840645-Phylogeny,
pubmed-meshheading:15840645-Plant Proteins,
pubmed-meshheading:15840645-Recombinant Fusion Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
The lysine-rich arabinogalactan-protein subfamily in Arabidopsis: gene expression, glycoprotein purification and biochemical characterization.
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pubmed:affiliation |
Department of Environmental and Plant Biology, Ohio University, Athens, OH 45701-2979, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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