Linked Life Data

16412428

Source:http://linkedlifedata.com/resource/pubmed/id/16412428

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-1-20
pubmed:abstractText
atToc33 is a transit peptide receptor of the chloroplast outer envelope membrane, and possesses GTPase activity. In vitro, its transit peptide- and GTP-binding properties are abrogated by its phosphorylation at serine 181, which was proposed to represent an important regulatory mechanism. We mutated S181 to alanine (to prevent phosphorylation), and to aspartate and glutamate (to mimic the effects of phosphoserine), and expressed all three proteins in ppi1 (atToc33 knockout) plants using the native promoter. The mutants complemented ppi1 with equal efficiency in respect of all criteria tested, including protein import efficiency and light stress tolerance. The data suggest that atToc33 phosphorylation may not play an important role in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
580
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
649-55
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
In vivo assessment of the significance of phosphorylation of the Arabidopsis chloroplast protein import receptor, atToc33.
pubmed:affiliation
Department of Plant and Environmental Sciences, Göteborg University, Box 461, SE-405 30 Göteborg, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't