Bc, Black cells, Mox, proPO-A1, Black cell
Gene model reviewed during 5.50
There is only one protein coding transcript and one polypeptide associated with this gene
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\PPO1 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\PPO1 in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for merge of: PPO1 Bc
The Bc (Black cells) mutation (FBal0001073) is a gain-of-function mutation in the PPO1 (CG42639) gene. The A480V lesion in PPO1 which is found in the Bc mutant allele is necessary and sufficient to phenocopy both the dominant Bc phenotype of spontaneously melanised crystal cells and the recessive Bc phenotype of defective melanisation after wounding. This indicates that the A480V lesion is the causal mutation of the Black cells phenotype and that Bc is allelic to PPO1.
"Phox" may correspond to "proPO-A1", since they map to the same location and both show monophenol oxidase activity.
PPO1 and PPO2 are the main source of phenoloxidase (PO) activity in the hemolymph (double mutants show no hemolymphatic PO activity upon wounding or after microbial infection). The two genes are not fully redundant: PPO1 is involved in the rapid early delivery of phenoloxidase activity when it is required, while PPO2 protein is accumulated in the crystals of crystal cells and provides a storage form that can be deployed in a second phase. PPO1 and PPO2 have a role in the survival of infection with Gram-positive bacteria and fungi.
Males have a minimum level of phenol oxidase activity that protects them from mechanical damage of cuticle or toxic effects. Females have high levels of phenol oxidase, may be caused by their reproductive function.
Mutants in Bc cause the loss of prophenoloxidase activity. Encapsulation of eggs from the parasitoid strain L.boulardi demonstrate that phenoloxidases are required only for blackening and hardening of haemolytic capsules.
The primary defect in Bc mutants may involve the loss of the physical barrier between phenol oxidase and its substrate in the crystal cells, which results in the melanisation of the cells in the mutant.
Phenol oxidase activity is reduced in heterozygous larval cell-free extracts and undetectable in homozygous larval cell-free extracts.