Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-7-20
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
A novel aspartic proteinase is targeted to the secretory pathway and to the vacuole in the moss Physcomitrella patens.
pubmed:affiliation
Plant Biotechnology, University of Freiburg, Freiburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't