Human clonorchiasis, caused by infection with the trematode Clonorchis sinensis, is a common health problem in East Asia. In an attempt to develop a new, sensitive method for the diagnosis of the disease, the use of a real-time PCR (targeting the internal-transcribed-spacer-2 sequence of the parasite) to detect C. sinensis-specific DNA in faecal samples has recently been evaluated. The PCR-based assay, which included an internal control to detect any inhibition of the amplification by faecal constituents in the sample, was performed on stool samples and on DNA controls representing a wide range of intestinal microorganisms. The assay appeared very specific, only showing positivity with C. sinensis and Opisthorchis felineus. The sensitivity of the assay was explored by testing 170 preselected samples of human faeces, from an endemic area of South Korea, which had known (microscopically-determined) densities of C. sinensis eggs. The sensitivity of the assay was 100% for the 74 samples that each had > 100 eggs/g and 91.4% for the other 70 samples found egg-positive by microcopy (i.e. those that had
Rph1, a Cys2-His2 zinc finger protein, binds to an upstream repressing sequence of the photolyase gene PHR1, and represses its transcription in response to DNA damage in Saccharomyces cerevisiae. In this report, we have demonstrated that the phosphorylation of Rph1 protein was increased in response to DNA damage. The DNA damage-induced phosphorylation of Rph1 was missing in most damage checkpoint mutants including rad9, rad17, mec1 and rad53. These results indicate that Rph1 phosphorylation is under the control of the Mec1-Rad53 damage checkpoint pathway. Rph1 phosphorylation required the kinase activity of Rad53 since it was significantly decreased in rad53 checkpoint mutant. Furthermore, loss of other kinases including Dun1, Tel1 and Chk1, which function downstream of Mec1, did not affect the Rph1 phosphorylation. This contrasts with the derepression of Crt1-regulated genes, which requires both Rad53 and Dun1 protein kinases. These results imply that posttranslational modification of Rph1 repressor is regulated by a potentially novel damage checkpoint pathway that is distinct from the RAD53-DUN1-CRT1 cascade implicated in the DNA damage-dependent transcription of ribonucleotide reductase genes.
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