Аннотация
Special AT-rich binding protein 1 (SATB1), a cell type-specific nuclear
matrix attachment region (MAR) DNA-binding protein, tethers to a
specific DNA sequence and regulates gene expression through chromatin
remodeling and HDAC (histone deacetylase complex) recruitment. In
this study, a SATB1 eukaryotic expression plasmid was transfected
into the human erythroleukemia K562 cell line and individual clones
that stably over-expressed the SATB1 protein were isolated. Microarray
analysis revealed that hundreds of genes were either up- or down-regulated
in the SATB1 over-expressing K562 cell lines. One of these was the
extra-cellular matrix glycoprotein, SPARC (human secreted protein
acidic and rich in cysteine). siRNA knock-down of SATB1 also reduced
SPARC expression, which was consistent with elevated SPARC levels
in the SATB1 over-expressing cell line. Bioinformatics software Mat-inspector
showed that a 17bp DNA sequence in the third intron of SPARC possessed
a high potential for SATB1 binding; a finding confirmed by Chromatin
immunoprecipitation (ChIP) with anti-SATB1 antibody. Our results
show for the first time that forced-expression of SATB1 in K562 cells
triggers SPARC up-regulation by binding to a 17bp DNA sequence in
the third intron.
Пользователи данного ресурса
Пожалуйста,
войдите в систему, чтобы принять участие в дискуссии (добавить собственные рецензию, или комментарий)