Source:http://linkedlifedata.com/resource/pubmed/id/19671704
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
43
|
pubmed:dateCreated |
2009-10-19
|
pubmed:abstractText |
Phytochromes are a collection of bilin-containing photoreceptors that regulate a diverse array of processes in microorganisms and plants through photoconversion between two stable states, a red light-absorbing Pr form, and a far red light-absorbing Pfr form. Recently, a novel set of phytochrome-like chromoproteins was discovered in cyanobacteria, designated here as cyanochromes, that instead photoconvert between stable blue and green light-absorbing forms Pb and Pg, respectively. Here, we show that the distinctive absorption properties of cyanochromes are facilitated through the binding of phycocyanobilin via two stable cysteine-based thioether linkages within the cGMP phosphodiesterase/adenyl cyclase/FhlA domain. Absorption, resonance Raman and infrared spectroscopy, and molecular modeling of the Te-PixJ GAF (cGMP phosphodiesterase/adenyl cyclase/FhlA) domain assembled with phycocyanobilin are consistent with attachments to the C3(1) carbon of the ethylidene side chain and the C4 or C5 carbons in the A-B methine bridge to generate a double thioether-linked phycoviolobilin-type chromophore. These spectroscopic methods combined with NMR data show that the bilin is fully protonated in the Pb and Pg states and that numerous conformation changes occur during Pb --> Pg photoconversion. Also identified were a number of photochromically inactive mutants with strong yellow or red fluorescence that may be useful for fluorescence-based cell biological assays. Phylogenetic analyses detected cyanochromes capable of different signaling outputs in a wide range of cyanobacterial species. One unusual case is the Synechocystis cyanochrome Etr1 that also binds ethylene, suggesting that it works as a hybrid receptor to simultaneously integrate light and hormone signals.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Algal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Phycobilins,
http://linkedlifedata.com/resource/pubmed/chemical/Phycocyanin,
http://linkedlifedata.com/resource/pubmed/chemical/phycocyanobilin,
http://linkedlifedata.com/resource/pubmed/chemical/phycoviolobilin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
1083-351X
|
pubmed:author |
pubmed-author:CornilescuClaudiaC,
pubmed-author:CornilescuGabrielG,
pubmed-author:HildebrandtPeterP,
pubmed-author:RiveraMarioM,
pubmed-author:StankeyRobert JRJ,
pubmed-author:UlijaszAndrew TAT,
pubmed-author:Velazquez EscobarFranciscoF,
pubmed-author:VierstraRichard DRD,
pubmed-author:ZhangJunruiJ,
pubmed-author:von StettenDavidD
|
pubmed:issnType |
Electronic
|
pubmed:day |
23
|
pubmed:volume |
284
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
29757-72
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:19671704-Algal Proteins,
pubmed-meshheading:19671704-Arabidopsis,
pubmed-meshheading:19671704-Arabidopsis Proteins,
pubmed-meshheading:19671704-Bacterial Proteins,
pubmed-meshheading:19671704-Cyanobacteria,
pubmed-meshheading:19671704-Cysteine,
pubmed-meshheading:19671704-Eukaryota,
pubmed-meshheading:19671704-Phycobilins,
pubmed-meshheading:19671704-Phycocyanin,
pubmed-meshheading:19671704-Protein Structure, Tertiary
|
pubmed:year |
2009
|
pubmed:articleTitle |
Cyanochromes are blue/green light photoreversible photoreceptors defined by a stable double cysteine linkage to a phycoviolobilin-type chromophore.
|
pubmed:affiliation |
Department of Genetics, University of Wisconsin, Madison, WI 53706, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|