The
            <i>Phycomyces madA</i>
            gene encodes a blue-light photoreceptor for phototropism and other light responses

Idnurm, Alexander; Rodríguez‐Romero, Julio; Corrochano, Luis M.; Sanz, Catalina; Iturriaga, Enrique A.; Eslava, Arturo P.; Heitman, Joseph

doi:10.1073/pnas.0600633103

Cited by 129 publications

(140 citation statements)

References 58 publications

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“…Strains with mutations in madA or madB had a mild defect in light-dependent cryA mRNA accumulation. Similar mild effects on photoactivation of transcription have been observed for other Phycomyces genes and are probably due to the high intensity of light that is applied and to the fact that none of them is a complete knockout (31,32). However, the double mutant strains did not show any accumulation of cryA mRNA after light exposure (Fig.…”

Section: Resultsmentioning

confidence: 53%

“…The perception of light in Phycomyces requires the products of the madA and madB genes that interact to form a photoreceptor complex (31,32). Strains with mutations in madA or madB had a mild defect in light-dependent cryA mRNA accumulation.…”

Section: Resultsmentioning

confidence: 99%

“…Phycomyces senses blue light through the action of the Mad complex, a homolog of the WC complex in N. crassa (31,32). Other elements of the signal transduction pathway for the phototropism of the fruiting body have been identified by mutations, but the corresponding mad genes remain to be identified (33).…”

Section: Significancementioning

confidence: 99%

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Fungal cryptochrome with DNA repair activity reveals an early stage in cryptochrome evolution

Tagua

Pausch

Eckel

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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DASH (Drosophila, Arabidopsis, Synechocystis, Human)-type cryp- tochromes (cry-DASH) belong to a family of flavoproteins acting as repair enzymes for UV-B–induced DNA lesions (photolyases) or as UV-A/blue light photoreceptors (cryptochromes). They are present in plants, bacteria, various vertebrates, and fungi and were originally considered as sensory photoreceptors because of their incapability to repair cyclobutane pyrimidine dimer (CPD) lesions in duplex DNA. However, cry-DASH can repair CPDs in single-stranded DNA, but their role in DNA repair in vivo remains to be clarified. The genome of the fungus Phycomyces blakesleeanus contains a single gene for a protein of the cryptochrome/photolyase family (CPF) encoding a cry-DASH, cryA, despite its ability to photoreactivate. Here, we show that cryA expression is induced by blue light in a Mad complex-dependent man- ner. Moreover, we demonstrate that CryA is capable of binding flavin (FAD) and methenyltetrahydrofolate (MTHF), fully complements the Escherichia coli photolyase mutant and repairs in vitro CPD lesions in single-stranded and double-stranded DNA with the same efficiency. These results support a role for Phycomyces cry-DASH as a photolyase and suggest a similar role for cry-DASH in mucoromycotina fung

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Section: Resultsmentioning

confidence: 53%

Section: Resultsmentioning

confidence: 99%

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Fungal cryptochrome with DNA repair activity reveals an early stage in cryptochrome evolution

Tagua

Pausch

Eckel

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…WC proteins have been well characterized in the filamentous ascomycete Neurospora crassa (Ballario et al, 1996;Linden and Macino, 1997;Froehlich et al, 2002;He et al, 2002), and homologues have been identified in ascomycetes, basidiomycetes, and zygomycetes (for review, see Corrochano, 2007). For example, Phycomyces blakesleeanus mutants defective in blue-light-dependent phototrophism may contain mutations in the madA gene, which encodes a protein similar to WC-1 of N. crassa (Idnurm et al, 2006). Inactivation of a wc-1 homologue in the human pathogen Cryptococcus neoformans results in a blind phenotype (Idnurm and Heitman, 2005;Lu et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

More Than a Repair Enzyme:Aspergillus nidulansPhotolyase-like CryA Is a Regulator of Sexual Development

Bayram

Biesemann

Krappmann

et al. 2008

MBoC

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Cryptochromes are blue-light receptors that have presumably evolved from the DNA photolyase protein family, and the genomes of many organisms contain genes for both types of molecules. Both protein structures resemble each other, which suggests that light control and light protection share a common ancient origin. In the genome of the filamentous fungus Aspergillus nidulans, however, only one cryptochrome/photolyase-encoding gene, termed cryA, was identified. Deletion of the cryA gene triggers sexual differentiation under inappropriate culture conditions and results in upregulation of transcripts encoding regulators of fruiting body formation. CryA is a protein whose N-and C-terminal synthetic green fluorescent protein fusions localize to the nucleus. CryA represses sexual development under UVA 350-370 nm light both on plates and in submerged culture. Strikingly, CryA exhibits photorepair activity as demonstrated by heterologous complementation of a DNA repair-deficient Escherichia coli strain as well as overexpression in an A. nidulans uvsB⌬ genetic background. This is in contrast to the single deletion cryA⌬ strain, which does not show increased sensitivity toward UV-induced damage. In A. nidulans, cryA encodes a novel type of cryptochrome/photolyase that exhibits a regulatory function during light-dependent development and DNA repair activity. This represents a paradigm for the evolutionary transition between photolyases and cryptochromes. INTRODUCTIONCryptochromes (CRYs) are blue-light receptors that regulate growth, development, and the circadian clock in higher eukaryotes and that are believed to have evolved from the DNA photolyase protein family (Daiyasu et al., 2004;Lin and Todo, 2005). Photolyases, in contrast, repair UV-induced DNA damage by using a mechanism referred to as photorepair. They absorb light in the blue spectrum and transfer an excited electron from the cofactor FAD to an enzyme-bound cyclobutane pyrimidine dimer (CPD), which is thereby cleaved (Sancar, 1990(Sancar, , 1994Sancar, 1994). Cryptochromes are characterized by an N-terminal photolyase-related (PHR) region without significant photorepair activity and by a C-terminal domain of varying length, which is absent in members of the CRY-DASH subfamily (Daiyasu et al., 2004). The exact function of the CRY-DASH proteins was elusive; however, recent data imply that they are actually photolyases that specifically repair CPDs in single-stranded DNA (Selby and Sancar, 2006). The PHR domain is the most conserved region of the CRY proteins and contains the cofactor FAD required for electron transfer reactions. In Xenopus and Drosophila, the PHR domain is physiologically active even in the absence of the C-terminal domain. The C-terminal domain is important for either localization or protein stability, and its expression in Arabidopsis results in constitutive growth (Lin and Todo, 2005). Plant CRYs are phosphorylated under illumination, and gene expression control ranges from protein interactions to direct chromatin interactions (Shalitin et al....

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“…The WC-2 protein contains a zinc-finger and 1 PAS domain (17), and interacts with WC-1 to form a complex that binds to the promoters of light-inducible genes, presumably to activate their transcription (13,18,19). WC proteins are required for the responses to blue light in the basidiomycete fungi Cryptococcus neoformans (20,21) and Coprinus cinereus (22), and 3 wc-1 genes have been described in the zygomycetes Rhizopus oryzae and Mucor circinelloides (23,24). A Mucor WC-1 protein is modified by ubiquitylation, presumably to regulate its activity (25).…”

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confidence: 99%

PhycomycesMADB interacts with MADA to form the primary photoreceptor complex for fungal phototropism

Sanz

Rodríguez‐Romero

Idnurm

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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The fungus Phycomyces blakesleeanus reacts to environmental signals, including light, gravity, touch, and the presence of nearby objects, by changing the speed and direction of growth of its fruiting body (sporangiophore). Phototropism, growth toward light, shares many features in fungi and plants but the molecular mechanisms remain to be fully elucidated. Phycomyces mutants with altered phototropism were isolated Ϸ40 years ago and found to have mutations in the mad genes. All of the responses to light in Phycomyces require the products of the madA and madB genes. We showed that madA encodes a protein similar to the Neurospora blue-light photoreceptor, zinc-finger protein WC-1. We show here that madB encodes a protein similar to the Neurospora zinc-finger protein WC-2. MADA and MADB interact to form a complex in yeast 2-hybrid assays and when coexpressed in E. coli, providing evidence that phototropism and other responses to light are mediated by a photoresponsive transcription factor complex. The Phycomyces genome contains 3 genes similar to wc-1, and 4 genes similar to wc-2, many of which are regulated by light in a madA or madB dependent manner. We did not detect any interactions between additional WC proteins in yeast 2-hybrid assays, which suggest that MADA and MADB form the major photoreceptor complex in Phycomyces. However, the presence of multiple wc genes in Phycomyces may enable perception across a broad range of light intensities, and may provide specialized photoreceptors for distinct photoresponses.blue light ͉ LOV domain ͉ White Collar protein ͉ zinc finger ͉ gene duplication

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The Phycomyces madA gene encodes a blue-light photoreceptor for phototropism and other light responses

Cited by 129 publications

References 58 publications

Fungal cryptochrome with DNA repair activity reveals an early stage in cryptochrome evolution

Fungal cryptochrome with DNA repair activity reveals an early stage in cryptochrome evolution

More Than a Repair Enzyme:Aspergillus nidulansPhotolyase-like CryA Is a Regulator of Sexual Development

PhycomycesMADB interacts with MADA to form the primary photoreceptor complex for fungal phototropism

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