The purine-rich element-binding protein ChPur-? negatively regulates Hsc70 transcription in Crassostrea hongkongensis.

ABSTRACT: ChPur-?, a purine-rich element-binding protein, was discovered showing affinity to the ChHsc70 promoter in Crassostrea hongkongensis by DNA affinity purification and mass spectrometry analysis. Direct interaction between purified ChPur-? and the ChHsc70 promoter region was demonstrated by electrophoretic mobility shift assay in vitro. ChPur-? reduction led to clear enhancements of ChHsc70 transcription in the hemocytes of C. hongkongensis. Consistently, ChPur-? overexpression in heterologous HEK293T cells correlated with repressive phenotype in ChHsc70 promoter expression. ChHsc70 transcription was responsive to heat shock or CdCl2 stress by RT-PCR, signifying an inducible feature of ChHsc70 transcription by physical/chemical stress despite its constitutive nature. ChPur-? transcription was also induced by the two stressors. This indicates a plausible association between ChHsc70 and ChPur-? in the stress-induced genetic regulatory pathway. This study discovered a negatively regulatory role of ChPur-? in controlling ChHsc70 transcription in C. hongkongensis, and contributed to better understanding the regulatory mechanisms in control of Hsc70 transcription.

SUBMITTER: Xu D 

PROVIDER: S-EPMC5741584 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature