Linked Life Data

12459457

Source:http://linkedlifedata.com/resource/pubmed/id/12459457

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-12-2
pubmed:abstractText
Regulation of tetrapyrrole biosynthesis in plants has been attributed to feedback control of glutamyl-tRNA reductase (GLU-TR) by heme. Recently, another negative regulator, the FLU protein, has been discovered that operates independently of heme. A truncated form of FLU that contains two domains implicated in protein-protein interaction was co-expressed in yeast with either GLU-TR or glutamate-1-semialdehyde-2-1-aminotransferase (GSA-AT), the second enzyme involved in delta-aminolevulinic acid (ALA) biosynthesis. FLU interacts strongly with GLU-TR but not with GSA-AT. Two variants of FLU that carry single amino acid exchanges within their coiled coil and tetratricopeptide repeat (TPR) domains, respectively, were also tested. Only the FLU variant with the mutated TPR motif lost the capacity to interact with GLU-TR.
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-30
pubmed:dateRevised
2006-11-15
pubmed:articleTitle
Interaction of FLU, a negative regulator of tetrapyrrole biosynthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU.
pubmed:affiliation
Institute of Plant Sciences, Swiss Federal Institute of Technology (ETH), Universitätstr. 2, 8092 Zürich, Switzerland.