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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2017.05.021
|2 doi
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|a pubmed25n0909.xml
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|a (DE-627)NLM272980978
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|a (NLM)28619534
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|a (PII)S0176-1617(17)30149-9
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Kottke, Tilman
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Cryptochrome photoreceptors in green algae
|b Unexpected versatility of mechanisms and functions
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 14.03.2018
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|a Date Revised 09.01.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2017 Elsevier GmbH. All rights reserved.
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|a Green algae have a highly complex and diverse set of cryptochrome photoreceptor candidates including members of the following subfamilies: plant, plant-like, animal-like, DASH and cryptochrome photolyase family 1 (CPF1). While some green algae encode most or all of them, others lack certain members. Here we present an overview about functional analyses of so far investigated cryptochrome photoreceptors from the green algae Chlamydomonas reinhardtii (plant and animal-like cryptochromes) and Ostreococcus tauri (CPF1) with regard to their biological significance and spectroscopic properties. Cryptochromes of both algae have been demonstrated recently to be involved to various extents in circadian clock regulation and in Chlamydomonas additionally in life cycle control. Moreover, CPF1 even performs light-driven DNA repair. The plant cryptochrome and CPF1 are UVA/blue light receptors, whereas the animal-like cryptochrome responds to almost the whole visible spectrum including red light. Accordingly, plant cryptochrome, animal-like cryptochrome and CPF1 differ fundamentally in their structural response to light as revealed by their visible and infrared spectroscopic signatures, and in the role of the flavin neutral radical acting as dark form or signaling state
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|a Journal Article
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|a Review
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|a Chlamydomonas reinhardtii
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|a Cryptochrome
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|a Flavin
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|a Green algae
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| 650 |
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|a Ostreococcus tauri
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| 650 |
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|a Photolyase
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| 650 |
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|a Cryptochromes
|2 NLM
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| 700 |
1 |
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|a Oldemeyer, Sabine
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wenzel, Sandra
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zou, Yong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mittag, Maria
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 217(2017) vom: 28. Okt., Seite 4-14
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
1 |
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|g volume:217
|g year:2017
|g day:28
|g month:10
|g pages:4-14
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| 856 |
4 |
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|u http://dx.doi.org/10.1016/j.jplph.2017.05.021
|3 Volltext
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|d 217
|j 2017
|b 28
|c 10
|h 4-14
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