Abstract
In this study, we examine the role of three highly conserved putative binding sites for Myc-associated zinc finger protein (MAZ) in regulation of the human SOX3 gene expression. Electrophoretic mobility shift and supershift assays indicate that complexes formed at two out of three MAZ sites of the human SOX3 promoter involve ubiquitously expressed MAZ protein. Furthermore, in cotransfection experiments we demonstrate that MAZ acts as a positive regulator of SOX3 gene transcription in both undifferentiated and RA-differentiated NT2/D1 cells. Although MAZ increased both basal and RA-induced promoter activity, our results suggest that MAZ does not contribute to RA inducibility of the SOX3 promoter during neuronal differentiation of NT2/D1 cells.
Highlights
The Sox proteins comprise a group of transcription factors that act as key regulators of cell fate decisions in diverse developmental events (Pevny and Lovell -Badge, 1997; We g n e r, 1999; Kamachi et al, 2000)
We further showed that the TATA box, Sp1, USF, and NF-Y binding sites within the basal promoter of the human SOX3 gene are of functional importance for its constitutive expression in embryonal carcinoma NT2/D1 cells (Kovacevic -Grujicic et al, 2005)
MatInspector analysis revealed three putative Myc-associated zinc finger protein (MAZ)-binding sites within the optimal promoter region of the human SOX3 gene positioned from -304 to -301, -52 to -49, and +213 to +216 relative to tsp. Comparative analysis of these putative human SOX3 regulatory regions with corresponding flanking sequences from chimpanzee (Pan troglodytes) and rhesus macaque (Macaca mullata) revealed that all three putative MAZ-binding sites are conserved with respect to their positions (Fig. 1A), while MAZ 2 and 3 are conserved with respect to the sequence as well
Summary
The Sox proteins comprise a group of transcription factors that act as key regulators of cell fate decisions in diverse developmental events (Pevny and Lovell -Badge , 1997; We g n e r , 1999; Kamachi et al, 2000). Sox transcription factors show both classical and architectural modes of action (Pevny and Lovell -Badge , 1997), either activating or repressing specific target genes through interaction with different partner proteins in a manner highly dependent on cell type and promoter context (Kamachi et al, 2000; Wilson and Koopman , 2002). They are characterized by the presence of a DNA-binding HMG domain (Pevny and Lovell -Badge , 1997; We g n e r , 1999) and classified into 10 groups (A - J) according to characteristics of the HMG domain and extraHMG domain sequences (Bowles et al, 2000). We show that exogenously added MAZ leads to an increase in SOX3 promoter activity in both undifferentiated and RAdifferentiated NT2/D1 cells
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