Linked Life Data

20419410

Source:http://linkedlifedata.com/resource/pubmed/id/20419410

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-4-26
pubmed:abstractText
Almost one-third of the proteins synthesized in the cytosol of cells ends up in membranes or outside the cell. Secretory polypeptides are synthesized as precursor proteins that carry N-terminal signal sequences. Secretion is catalyzed by the "translocase" that comprises a channel-clamp protein and an ATPase motor. Translocase activities have been fully reconstituted in vitro. This provided powerful tools to examine the role of each component in the reaction. Here we describe protocols for the purification of the secretory preprotein alkaline phosphatase and a series of in vitro assays developed in order to examine the binding of alkaline phosphatase to the translocase, its ability to stimulate ATP hydrolysis, and finally its transfer across the membrane. The assays are applicable to any similar study of secretory preproteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
619
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-72
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
In vitro assays to analyze translocation of the model secretory preprotein alkaline phosphatase.
pubmed:affiliation
Department of Biology, University of Crete and Institute of Molecular Biology and Biotechnology-Foundation for Research and Technology Hellas, Heraklion, Crete, Greece.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't