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| Title: Rice plastidial N-glycosylated nucleotide pyrophosphatase/phosphodiesterase is transported from the ER-golgi to the chloroplast through the secretory pathway .
| | Author: Nanjo Y Oka H Ikarashi N Kaneko K Kitajima A Mitsui T Muoz FJ Rodrguez-Lpez M Baroja-Fernndez E Pozueta-Romero J | | Journal: Plant Cell Citation: V : 18 ( 10 ) P : 2582-92 Year: 2006 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub17028208 Accession (PMID): 17028208 | | Abstract: A nucleotide pyrophosphatase/phosphodiesterase ( NPP ) activity that catalyzes the hydrolytic breakdown of ADP-glucose ( ADPG ) has been shown to occur in the plastidial compartment of both mono and dicotyledonous plants .
To learn more about this enzyme , we purified two NPPs from rice ( Oryza sativa ) and barley ( Hordeum vulgare ) seedlings .
Both enzymes are glycosylated , since they bind to concanavalin A , stain with periodic acid-Schiff reagent , and are digested by Endo-H A complete rice NPP cDNA , designated as NPP1 , was isolated , characterized , and overexpressed in transgenic plants displaying high ADPG hydrolytic activity .
Databank searches revealed that NPP1 belongs to a functionally divergent group of plant nucleotide hydrolases .
NPP1 contains numerous N-glycosylation sites and a cleavable hydrophobic signal sequence that does not match with the N-terminal part of the mature protein .
Both immunocytochemical analyses and confocal fluorescence microscopy of rice cells expressing NPP1 fused with green fluorescent protein ( GFP ) revealed that NPP1-GFP occurs in the plastidial compartment .
Brefeldin A treatment of NPP1-GFP-expressing cells prevented NPP1-GFP accumulation in the chloroplasts .
Endo-H digestibility studies revealed that both NPP1 and NPP1-GFP in the chloroplast are glycosylated .
Collectively , these data demonstrate the trafficking of glycosylated proteins from the endoplasmic reticulum-Golgi system to the chloroplast in higher plants . | Matching Sentences:
[ Sen. 6, subscore: 2.00 ]: Both immunocytochemical analyses and confocal fluorescence microscopy of rice cells expressing NPP1 fused with green fluorescent protein ( GFP ) revealed that NPP1-GFP occurs in the plastidial compartment .
[ Sen. 7, subscore: 2.00 ]: Brefeldin A treatment of NPP1-GFP-expressing cells prevented NPP1-GFP accumulation in the chloroplasts .
[ Sen. 8, subscore: 2.00 ]: Endo-H digestibility studies revealed that both NPP1 and NPP1-GFP in the chloroplast are glycosylated .
[ Sen. 3, subscore: 1.00 ]: Both enzymes are glycosylated , since they bind to concanavalin A , stain with periodic acid-Schiff reagent , and are digested by Endo-H A complete rice NPP cDNA , designated as NPP1 , was isolated , characterized , and overexpressed in transgenic plants displaying high ADPG hydrolytic activity .
[ Sen. 4, subscore: 1.00 ]: Databank searches revealed that NPP1 belongs to a functionally divergent group of plant nucleotide hydrolases .
[ Sen. 5, subscore: 1.00 ]: NPP1 contains numerous N-glycosylation sites and a cleavable hydrophobic signal sequence that does not match with the N-terminal part of the mature protein .
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