Source:http://linkedlifedata.com/resource/pubmed/id/15260436
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-7-20
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pubmed:databankReference | |
pubmed:abstractText |
In seed plants aspartic proteases (APs) are known to reside in storage vacuoles. Targeting to this compartment is provoked by a secretory signal peptide and the plant-specific insert (PSI). In order to study secretory and vacuolar targeting in a seedless plant, the moss Physcomitrella patens, we isolated a cDNA encoding PpAP1, a novel aspartic proteinase. Sequence alignment with other members of the family of plant APs (EC 3.4.23) revealed a high overall identity and the Pfam motifs for aspartic proteinase and PSI were clearly recognised. In phylogenetic analysis PpAP1 was placed at a very basal position outside of the bigger clusters. Protoplasts transiently expressing the PpAP1 signal peptide fused to GFP showed fluorescence in a well-developed ER-Golgi network. A C-terminal fusion of GFP to the entire PpAP1 protein showed vacuolar fluorescence in transiently transfected protoplasts. Therefore, the vacuole is apparently the in-vivo target for PpAP1. In this study the three-dimensional peculiarity of the endomembrane continuum of ER and Golgi was visualised in a seedless plant for the first time. Above all the functionality of the secretory and the vacuolar targeting signals make them become useful tools for biotechnological approaches.
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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/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0171-9335
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-52
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15260436-Amino Acid Sequence,
pubmed-meshheading:15260436-Aspartic Acid Endopeptidases,
pubmed-meshheading:15260436-Bryopsida,
pubmed-meshheading:15260436-Cloning, Molecular,
pubmed-meshheading:15260436-Green Fluorescent Proteins,
pubmed-meshheading:15260436-Intracellular Membranes,
pubmed-meshheading:15260436-Molecular Sequence Data,
pubmed-meshheading:15260436-Phylogeny,
pubmed-meshheading:15260436-Protein Sorting Signals,
pubmed-meshheading:15260436-Recombinant Fusion Proteins,
pubmed-meshheading:15260436-Secretory Vesicles,
pubmed-meshheading:15260436-Sequence Alignment,
pubmed-meshheading:15260436-Sequence Analysis, Protein,
pubmed-meshheading:15260436-Vacuoles
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pubmed:year |
2004
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pubmed:articleTitle |
A novel aspartic proteinase is targeted to the secretory pathway and to the vacuole in the moss Physcomitrella patens.
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pubmed:affiliation |
Plant Biotechnology, University of Freiburg, Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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