The analysis also divulged new actors of multi-drug resistance, whose transcription was activated owing to the differential occupancy of Ncb2.
The conditional, sequence-specific positional escape of Ncb2 from the core promoter in AS isolate and its preferential recruitment to the core promoter of certain genes in AR isolates was most noteworthy means of transcription regulation.
albicans, we performed a genome-wide recruitment analysis of the transcriptional regulator by employing Ch IP-on-chip assay and compared it between azole sensitive (AS) and AR isolates.
Three biological replicates were processed for each of the isolate to identify DNA regions that were occupied by Ncb2.
In an earlier report, we have shown the importance of the β-subunit of NC2 complex in the basal and activated transcription of CDR1 in azole sensitive (AS-Gu4) and azole resistant (AR-Gu5) isolates of C.
albicans and also provided evidence that this cofactor may also be involved in the regulation of select genes, particularly those targeted by Tac1.
Average binding profiles of Ncb2 for the promoter regions were determined relative to ATG start codon for both the isolates.
Green line represents localization profile of Ncb2 in the AS isolate; whereas blue line represents localization profile of Ncb2 in AR isolate.
albicans genes of almost every metabolic class in AR and AS isolates, thereby reinforcing its status as a global regulator of gene expression.
NC2 is a heterodimer comprised of two subunits, NC2α and NC2β (Ncb2) which was originally recognized as a TATA-binding protein (TBP) activity in human nuclear extracts that repressed RNA Pol II transcription.
Additionally, NC2 can localize TBP onto the promoters by using its histone fold domain and bind to the underside of the DNA by using C-terminal helix of NC2β which surrounds DNA and binds convex side of TBP.
Trans-acting factors regulating CDR1 have also been identified.
For example, Non dityrosine 80 (Ndt80), a homolog to a meiosis-specific transcription factor (TF) in Saccharomyces cerevisiae is an activator of CDR1.