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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1993-7-22
|
| pubmed:abstractText |
In vitro reconstitution assays have been used in recent years to probe the mechanisms by which a variety of cytosolically synthesised proteins are transported across the thylakoid membrane within higher plant chloroplasts. The emerging data suggest that two distinct mechanisms operate. Translocation of a subset of lumenal proteins, namely the 23 kDa and 16 kDa proteins of the oxygen-evolving complex, and of the CFo2 protein (an integral membrane protein), requires only the presence of the thylakoidal delta pH. In contrast, two other lumenal proteins, the 33 kDa oxygen-evolving complex protein and plastocyanin, require also the presence of ATP and at least one stromal factor for efficient transport into isolated thylakoids to take place.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
28
|
| pubmed:volume |
325
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
67-9
|
| pubmed:dateRevised |
2005-11-16
|
| pubmed:meshHeading | |
| pubmed:year |
1993
|
| pubmed:articleTitle |
Protein translocation across the thylakoid membrane--a tale of two mechanisms.
|
| pubmed:affiliation |
Department of Biological Sciences, University of Warwick, Coventry, UK.
|
| pubmed:publicationType |
Journal Article,
Review
|