Source:http://linkedlifedata.com/resource/pubmed/id/16966335
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
45
|
pubmed:dateCreated |
2006-11-6
|
pubmed:abstractText |
Phytochrome A (phyA) is a versatile plant photoreceptor that mediates responses to brief light exposures (very low fluence responses, VLFR) as well as to prolonged irradiation (high irradiance responses, HIR). We identified the phyA-303 mutant allele of Arabidopsis thaliana bearing an R384K substitution in the GAF subdomain of the N-terminal half of phyA. phyA-303 showed reduced phyA spectral activity, almost normal VLFR, and severely impaired HIR. Recombinant N-terminal half oat of PHYA bearing the phyA-303 mutation showed poor incorporation of chromophore in vitro, despite the predicted relatively long distance (>13 A) between the mutation and the closest ring of the chromophore. Fusion proteins bearing the N-terminal domain of oat phyA, beta-glucuronidase, green fluorescent protein, and a nuclear localization signal showed physiological activity in darkness and mediated VLFR but not HIR. At equal protein levels, the phyA-303 mutation caused slightly less activity than the fusions containing the wild-type sequence. Taken together, these studies highlight the role of the N-terminal domain of phyA in signaling and of distant residues of the GAF subdomain in the regulation of phytochrome bilin-lyase activity.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronidase,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PHYA protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Phytochrome A,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
281
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
34421-9
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:16966335-Arabidopsis,
pubmed-meshheading:16966335-Arabidopsis Proteins,
pubmed-meshheading:16966335-Cell Nucleus,
pubmed-meshheading:16966335-Darkness,
pubmed-meshheading:16966335-Glucuronidase,
pubmed-meshheading:16966335-Green Fluorescent Proteins,
pubmed-meshheading:16966335-Hypocotyl,
pubmed-meshheading:16966335-Light,
pubmed-meshheading:16966335-Mutation,
pubmed-meshheading:16966335-Photoreceptor Cells,
pubmed-meshheading:16966335-Phytochrome A,
pubmed-meshheading:16966335-Plants, Genetically Modified,
pubmed-meshheading:16966335-Protein Structure, Tertiary,
pubmed-meshheading:16966335-Protein Transport,
pubmed-meshheading:16966335-Recombinant Fusion Proteins,
pubmed-meshheading:16966335-Seeds,
pubmed-meshheading:16966335-Signal Transduction
|
pubmed:year |
2006
|
pubmed:articleTitle |
Functional and biochemical analysis of the N-terminal domain of phytochrome A.
|
pubmed:affiliation |
Max-Planck-Institut für Bioanorganische Chemie, Postfach 101356, D-45413 Mülheim an der Ruhr, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|