Identification of a New Cryptochrome Class

Brudler, Ronald; Hitomi, Katsundo; Daiyasu, Hiromi; Toh, Hiroyuki; Kucho, Ken-ichi; Ishiura, Masahiro; Kanehisa, Minoru; Roberts, Victoria A.; Todo, Tomoki; Tainer, John A.; Getzoff, Elizabeth D.

doi:10.1016/s1097-2765(03)00008-x

Cited by 293 publications

(422 citation statements)

References 37 publications

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“…When this strain was complemented, illumination increased the survival to 67 %, similar to that of the complemented phrA mutant. Selby & Sancar (2006) reported recently that members of the previously found cryptochrome DASH family (Brudler et al, 2003;Daiyasu et al, 2004) repair single stranded DNA. Although RSP3077 shows only minor (up to 9 %) sequence identity to members of this family, we can not exclude a function of RSP3077 in this regard and a role as putative second photolyase.…”

Section: Resultsmentioning

confidence: 99%

“…(Tamada et al, 1997;top line) and Synechocystis sp. PCC6803 (Brudler et al, 2003;bottom line). The black boxed tryptophans are believed to be involved in intraprotein electron transport (Byrdin et al, 2003).…”

Section: Methodsmentioning

confidence: 99%

“…Cry, cryptochrome DASH of Synechocystis sp. PCC6803 (Brudler et al, 2003). Comparison was carried out using MultAlin software (http://prodes.toulouse.inra.fr/multalin/multalin.html).…”

Section: Methodsmentioning

confidence: 99%

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The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a σ E-dependent manner

et al. 2007

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a σ E-dependent manner

et al. 2007

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“…Certainly the presence of five phytochromes, two cryptochromes, two phototropins, and three other LOV domain receptors suggest the plant light sensor collection coordinates a complex circuit of integrated responses that are dependent upon plant developmental state, tissue, or cell type. Add to this the noted and potential light-sensing roles for zeaxanthin (Frechilla et al, 2000;Talbott et al, 2003), cry-DASH (Brudler et al, 2003), G proteins (Warpeha et al, 1991), and possibly flavinbinding aquaporins (Lorenz et al, 2003) and it is clear that there are many additional candidates that may be modulating the GL plastid response. It also is of interest to determine how the developmentally contrary GL effects integrate with the inductive photomorphogenic responses associated with blue and red wavebands.…”

Section: Discussionmentioning

confidence: 99%

Green Light Adjusts the Plastid Transcriptome during Early Photomorphogenic Development

et al. 2006

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During the transition from darkness to light, a suite of light sensors guides gene expression, biochemistry, and morphology to optimize acclimation to the new environment. Ultraviolet, blue, red, and far-red light all have demonstrated roles in modulating light responses, such as changes in gene expression and suppression of stem growth rate. However, green wavebands induce stem growth elongation, a response not likely mediated by known photosensors. In this study, etiolated Arabidopsis (Arabidopsis thaliana) seedlings were treated with a short, dim, single pulse of green light comparable in fluence and duration to that previously shown to excite robust stem elongation. Genome microarrays were then used to monitor coincident changes in gene expression. As anticipated, phytochrome A-regulated, nuclear-encoded transcripts were induced, confirming proper function of the sensitive phytochrome system. In addition, a suite of plastid-encoded transcripts decreased in abundance, including several typically upregulated after phytochrome and/or cryptochrome activation. Further analyses using RNA gel-blot experiments demonstrated that the response is specific to green light, fluence dependent, and detectable within 30 min. The response obeys reciprocity and persists in the absence of known photosensors. Plastid transcript down-regulation was also observed in tobacco (Nicotiana tabacum) with similar temporal and fluence-response kinetics. Together, the down-regulation of plastid transcripts and increase in stem growth rate represent a mechanism that tempers progression of early commitment to the light environment, helping tailor seedling development during the critical process of establishment.

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“…Interestingly, the cluster is just at the rim of the FADcontaining cavity. FAD is essential in the repair reaction of DNA photolyase (22,39,42) that occurs by electron transfer from light-excited FADHϪ to the UV-induced DNA lesion. This reaction is initiated by entrance of the damaged site into the hole, providing access to the FAD bound at the bottom of the cavity.…”

Section: Discussionmentioning

confidence: 99%

Functional and Structural Analyses of Cryptochrome

Hirayama

Nakamura

Ishikawa

et al. 2003

Journal of Biological Chemistry

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Mouse mCRY1 and zebrafish zCRY1a and zCRY3 belong to the DNA photolyase/Cryptochrome family. mCRY1 and zCRY1a repress CLOCK:BMAL1-mediated transcription, whereas zCRY3 does not. Reciprocal chimeras between zCRY1a and zCRY3 were generated to determine the zCRY1a regions responsible for nuclear translocation, interaction with the CLOCK:BMAL1 heterodimer, and repression of CLOCK:BMAL1-mediated transcription. Three regions, RD-2a-(126 -196), RD-1-(197-263), and RD-2b-(264 -293), were identified. Proteins in this family consist of an N-terminal ␣/␤ domain and a C-terminal helical domain connected by an interdomain loop. RD-2a is within this loop, RD-1 is at the N-terminal 50 amino acids, and RD-2b at the following 31 amino acid residues of the helical domain. Either RD-2a or RD-1 is required for interaction with the CLOCK: BMAL1 heterodimer, and either RD-1 or RD-2b is required for the nuclear translocation of CRY. Both of these functions are prerequisites for the transcriptional repressor activity. The functional nuclear localizing signal in the RD-2b region also was identified. The sequence is well conserved among repressor-type CRYs, including mCRY1. Mutations in the nuclear localizing signal of mCRY1 reduce the extent of its nuclear localization. These findings show that both nuclear localization and interaction with the CLOCK:BMAL heterodimer are essential for transcriptional repression by CRY.Organisms ranging from bacteria to humans have daily rhythms driven by endogenous oscillators called circadian clocks that regulate various biochemical, physiological, and behavioral processes with a periodicity of approximate by 24 h (1-3). Under natural conditions, rhythms are entrained to a 24-h day by environmental time cues, most commonly light. These circadian clock mechanisms have been investigated by characterizing the "clock genes" that affect the daily rhythm. The core of the clock mechanisms in Drosophila, Neurospora, mammals, and cyanobacteria is expressed by a transcription/ translation-based negative feedback loop that relies on positive and negative oscillator elements. The negative feedback loop begins by activating the transcription of clock genes, the products of which then negatively regulate their own expression, setting up the rhythmic oscillations of gene expression that drive the circadian clock. Although negative feedback loop is a common mechanism in Drosophila, Neurospora, mammals, and cyanobacteria, its components differ with the species. Drosophila and mammals have common components (orthologous gene products), except for the negative elements TIM 1 (TIMELESS) and CRY (Cryptochrome). PER (PERIOD), and TIM, identified as the negative elements in Drosophila, form a heterodimer that translocates to the nucleus where its components interact with the positive elements dCLOCK and CYC (4). Formation of a complex decreases dCLOCK:CYC-mediated transcription, resulting in the repression of expression (5, 6). In mammals, CRY1 and CRY2 are partners of the PER heterodimer, rather than TIM. In mammals, the mP...

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Identification of a New Cryptochrome Class

Cited by 293 publications

References 37 publications

The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a σ E-dependent manner

The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a σ E-dependent manner

Green Light Adjusts the Plastid Transcriptome during Early Photomorphogenic Development

Functional and Structural Analyses of Cryptochrome

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