Article Abstract:
Mad1 forms a complex with mSin3A and HDAC as evidenced by immunoprecipation by using [S]methionine-labeled 293epithelial cells. HDAC and Mad bind to separate regions of mSin3 as proved by using immunoprecipitation and transfection of 293 with plasmids expressing Mad1, HA-tagged Mad1, and HA-tagged Mad3. Mad1 repression requires histone deacetylase activity through formation of a ternary comlex with mSin3A and HDAC1/2 as proved by the effect of a specific histone deacetylase inhibitor on Mad1 transcriptional activity.
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Article Abstract:
Previous research have failed to fully explain the role of linker histone in transcription in vivo. One way to remedy this problem is to look at Tetrahymena thermophila, a model system which provides a unique opportunity for elucidating on the linker histone function. Experiments show that the linker histone H1 knockout strain of Tetrahymena thermophila has no major effect on global transcription, although it acts as either a positive or negative gene-specific regulator of transcription in vivo.
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Article Abstract:
A study was performed to demonstrate that the serum-resistance-associated (SRA) gene is an expression site-associated gene of the Edinburgh trypanozoon antigen type 1.10 (ETat 1.10) expression site. The SRA gene was encoded a variant surface glycoprotein-like protein and was only present in the R clones of the ETat strain of the Trypanosoma brucei rhodesiense resistant to normal human serum. Results revealed that SRA resulted to the resistance of the organism against normal human serum.
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