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Upregulation of Murine 1‐Cys Peroxiredoxin Gene by B Cell Activator Protein, Pax5
Author(s) -
Pak Jhang Ho,
Kim HanSuk,
Lee InSeon,
Choi WonHo,
Seo SangBeom
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a286-c
Subject(s) - pax5 , microbiology and biotechnology , biology , transcription factor , activator (genetics) , promoter , gene , dna binding protein , regulation of gene expression , gene expression , genetics
Pax5, a member of the paired box gene family of transcription factors, encodes the B cell specific activator protein (BSAP) that plays important roles in controlling the expression of lineage‐ and differentiation‐stage‐specific genes during B lymphopoiesis. We identified two putative Pax5 binding sites in a 668bp of the murine 1‐cys peroxiredoxin (1‐cysPrx) promoter region. These were located at positions −278 to −262 and −50 to −34 from the translation start sites. The gel mobility shift assay showed that recombinant Pax5 protein bound specifically to each probe spanning nucleotides −56 to −24 (MP1) and −284 to −253 (MP2). Furthermore, native Pax5 protein from B lymphoblast cells (IM‐9) formed DNA‐protein complex, indicating that in vivo Pax5‐binding occurred specifically at these sequences. 1‐cysPrx promoter‐luciferase vector (pGL‐mPx) and Pax5 expression vector (pcDNA‐Pax5) were transiently cotransfected to HeLa cells that did not express endogenous Pax5 protein. Pax5 increased the promoter activities up to ~12‐fold in a dose dependent manner, implying that Pax5 functions as a positive transcriptional factor for the 1‐cysPrx expression. These activities were further elevated with the presence of histone acetyltransferases (HAT), p300/CBP. Taken together, our results suggest that Pax5 can function as an important element to transactivate the expression of 1‐cysPrx gene. Supported by KOSEF (R01‐2006‐000‐11189‐02006).