Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.99.3 extracted from

  • Cohrs, K.; Schumacher, J.
    The two cryptochrome/photolyase family proteins fulfill distinct roles in DNA photorepair and regulation of conidiation in the gray mold fungus Botrytis cinerea (2017), Appl. Environ. Microbiol., 83, pii: e00812-17 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene bccry1, light-induced gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional recombinant expression of GFP-tagged enzyme BcCRY1-GFP in Botrytis cinerea, it restores the wild-type phenotype in the BcCRY1 deletion mutant Botrytis cinerea
gene bccry2, light-induced gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional recombinant expression of GFP-tagged enzyme GFP-BcCRY2 in Botrytis cinerea, it restores the wild-type phenotype in the BcCRY2 deletion mutant Botrytis cinerea

Protein Variants

Protein Variants Comment Organism
additional information generation of deletion mutant DELTAbccry1 and overexpression strain OE::bccry1, phenotype, overview Botrytis cinerea
additional information generation of deletion mutant DELTAbccry2 and overexpression strain OE::bccry2, phenotype, overview Botrytis cinerea

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Botrytis cinerea 5829
-
additional information no localization in nuclei Botrytis cinerea
-
-
nucleus exclusively Botrytis cinerea 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclobutadipyrimidine (in DNA) Botrytis cinerea
-
2 pyrimidine residues (in DNA)
-
?
cyclobutadipyrimidine (in DNA) Botrytis cinerea B05.10
-
2 pyrimidine residues (in DNA)
-
?

Organism

Organism UniProt Comment Textmining
Botrytis cinerea A0A384JIP4 i.e. Botrytis cinerea
-
Botrytis cinerea A0A384JRT3 i.e. Botrytis cinerea
-
Botrytis cinerea B05.10 A0A384JIP4 i.e. Botrytis cinerea
-
Botrytis cinerea B05.10 A0A384JRT3 i.e. Botrytis cinerea
-

Source Tissue

Source Tissue Comment Organism Textmining
conidium
-
Botrytis cinerea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine (in DNA)
-
Botrytis cinerea 2 pyrimidine residues (in DNA)
-
?
cyclobutadipyrimidine (in DNA)
-
Botrytis cinerea B05.10 2 pyrimidine residues (in DNA)
-
?

Subunits

Subunits Comment Organism
More BcCRY1 comprises an N-terminal DNA photolyase domain (Pfam accession no. PF00875) and a C-terminal FAD-binding domain (PF03441). Further sequence analysis predicts a nuclear localization signal (192KRKR195) in the DNA photolyase domain Botrytis cinerea
More BcCRY2 features a N-terminal DNA photolyase (PF00875) domain and a C-terminal FAD-binding (PF03441) domain, and contains an additional C-terminal R/G-rich region that is often associated with the ability to interact with RNA Botrytis cinerea

Synonyms

Synonyms Comment Organism
BcCRY1
-
Botrytis cinerea
BcCRY2
-
Botrytis cinerea
BCIN_05g08060
-
Botrytis cinerea
BCIN_09g01620
-
Botrytis cinerea
CPD photolyase
-
Botrytis cinerea
Cry1
-
Botrytis cinerea
cyclobutane pyrimidine dimer photolyase
-
Botrytis cinerea

Expression

Organism Comment Expression
Botrytis cinerea the transcription of bccry1 is induced by light in a White Collar complex (WCC)-dependent manner up
Botrytis cinerea the transcription of bccry2 is induced by light in a White Collar complex (WCC)-dependent manner, but neither light nor the WCC is essential for the repression of conidiation through BcCRY2 when bccry2 is constitutively expressed up

General Information

General Information Comment Organism
evolution the enzyme BcCRY1 belongs to the cryptochrome/photolyase family (CPF), CPD photolyase subfamily Botrytis cinerea
evolution the enzyme BcCRY2 belongs to the cryptochrome/photolyase family (CPF), cry-DASH subfamily Botrytis cinerea
malfunction no changes in UV tolerance and therefore in the effectiveness of photoreactivation are observed for bccry2 deletion or overexpression strains. A retarded lesion spreading, 75% of wild-type, is noted for overexpressing OE::bccry2 strains following inoculation with conidia, overabundance of BcCRY2 causes reduced radial growth rates and delayed initiation of vegetative growth of germinating conidia in axenic culture, and this effect occurs independently of the light conditions Botrytis cinerea
malfunction the DELTAbccry1 mutant is unable to grow after UV exposure for 6 min, absence of photoreactivation. Overexpression of bccry1 increases UV tolerance, OE::bccry1 conidia show more efficient photoreactivation than the wild-type. Reintroduction of bccry1 into the deficient DELTAbccry1 mutant restores the photorepair activity to wild-type levels. Neither deletion nor overexpression of bccry1 affects differentiation under the conditions tested, the strains show wild-type-like conidiation Botrytis cinerea
physiological function conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. BcCRY2 belongs to the cry-DASH proteins and is dispensable for photorepair but performs regulatory functions by repressing conidiation in white and especially black/NUV light. Neither light nor the White Collar complex (WCC) is essential for the repression of conidiation through BcCRY2 when bccry2 is constitutively expressed. BcCRY2 affects the transcript levels of both WCC-induced and WCC-repressed genes, suggesting a signaling function downstream of the WCC. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY2 acts as a cryptochrome with a signaling function in regulating photomorphogenesis (repression of conidiation). BcCRY2 functions in the regulation of vegetative growth, overview. BcCRY2 has a negative impact on conidiation, the R/G-rich region of BcCRY2 is not essential for the regulation of conidiation. No impact of BcCRY2 on sclerotial development Botrytis cinerea
physiological function conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. CRY1 (BcCRY1), a cyclobutane pyrimidine dimer (CPD) photolyase, acts as the major enzyme of light-driven DNA repair (photoreactivation) and has no obvious role in signaling. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY1 acts as the major photolyase in photoprotection, BcCRY1 is crucial for photorepair, overview. No impact of BcCRY1 on sclerotial development Botrytis cinerea