001     59358
005     20200402210430.0
024 7 _ |2 pmid
|a pmid:17548357
024 7 _ |2 DOI
|a 10.1074/jbc.M700849200
024 7 _ |2 WOS
|a WOS:000248196800019
037 _ _ |a PreJuSER-59358
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Immeln, D.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB72038
245 _ _ |a Blue Light Induces Radical Formation and Autophosphorylation in the Light-sensitive Domain of Chlamydomonas Cryptochrome
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2007
300 _ _ |a 21720 - 21728
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of Biological Chemistry
|x 0021-9258
|0 3091
|y 30
|v 282
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Cryptochromes are sensory blue light receptors mediating various responses in plants and animals. Studies on the mechanism of plant cryptochromes have been focused on the flowering plant Arabidopsis. In the genome of the unicellular green alga Chlamydomonas reinhardtii, a single plant cryptochrome, Chlamydomonas photolyase homologue 1 (CPH1), has been identified. The N-terminal 500 amino acids comprise the light-sensitive domain of CPH1 linked to a C-terminal extension of similar size. We have expressed the light-sensitive domain heterologously in Escherichia coli in high yield and purity. The 59-kDa protein bears exclusively flavin adenine dinucleotide in its oxidized state. Illumination with blue light induces formation of a neutral flavin radical with absorption maxima at 540 and 580 nm. The reaction proceeds aerobically even in the absence of an exogenous electron donor, which suggests that it reflects a physiological response. The process is completely reversible in the dark and exhibits a decay time constant of 200 s in the presence of oxygen. Binding of ATP strongly stabilizes the radical state after illumination and impedes the dark recovery. Thus, ATP binding has functional significance for plant cryptochromes and does not merely result from structural homology to DNA photolyase. The light-sensitive domain responds to illumination by an increase in phosphorylation. The autophosphorylation takes place although the protein is lacking its native C-terminal extension. This finding indicates that the extension is dispensable for autophosphorylation, despite the role it has been assigned in mediating signal transduction in Arabidopsis.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Chlamydomonas: physiology
650 _ 2 |2 MeSH
|a Chlamydomonas: radiation effects
650 _ 2 |2 MeSH
|a Cryptochromes
650 _ 2 |2 MeSH
|a DNA, Protozoan: genetics
650 _ 2 |2 MeSH
|a DNA, Protozoan: isolation & purification
650 _ 2 |2 MeSH
|a Escherichia coli: genetics
650 _ 2 |2 MeSH
|a Flavoproteins: genetics
650 _ 2 |2 MeSH
|a Flavoproteins: metabolism
650 _ 2 |2 MeSH
|a Flavoproteins: radiation effects
650 _ 2 |2 MeSH
|a Free Radicals
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Light Signal Transduction
650 _ 2 |2 MeSH
|a Phosphorylation
650 _ 2 |2 MeSH
|a Protozoan Proteins: metabolism
650 _ 2 |2 MeSH
|a Protozoan Proteins: radiation effects
650 _ 2 |2 MeSH
|a Recombinant Proteins: metabolism
650 _ 2 |2 MeSH
|a Recombinant Proteins: radiation effects
650 _ 7 |0 0
|2 NLM Chemicals
|a Cryptochromes
650 _ 7 |0 0
|2 NLM Chemicals
|a DNA, Protozoan
650 _ 7 |0 0
|2 NLM Chemicals
|a Flavoproteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Free Radicals
650 _ 7 |0 0
|2 NLM Chemicals
|a Protozoan Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |a J
|2 WoSType
700 1 _ |a Schlesinger, R.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB1421
700 1 _ |a Heberle, J.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Kottke, T.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB16784
773 _ _ |a 10.1074/jbc.M700849200
|g Vol. 282, p. 21720 - 21728
|p 21720 - 21728
|q 282<21720 - 21728
|0 PERI:(DE-600)1474604-9
|t The @journal of biological chemistry
|v 282
|y 2007
|x 0021-9258
856 7 _ |u http://dx.doi.org/10.1074/jbc.M700849200
909 C O |o oai:juser.fz-juelich.de:59358
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
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|x 0
914 1 _ |y 2007
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
|g INB
|0 I:(DE-Juel1)VDB805
|x 1
970 _ _ |a VDB:(DE-Juel1)93387
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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