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A Col9a1 enhancer element activated by two interdependent SOX9 dimers.

Mary Ann Genzer¹, Laura C Bridgewater

¹Department of Microbiology and Molecular Biology, Brigham Young University, Provo, Utah 84602, USA.

Nucleic Acids Research

|February 1, 2007

Summary

The transcription factor SOX9 activates genes by binding DNA. This study reveals a novel mechanism where two SOX9 dimers on the COL9A1 enhancer cooperate for transcriptional activation in chondrogenesis.

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Area of Science:

Molecular Biology
Developmental Biology
Genetics

Background:

SOX9 is a crucial transcription factor involved in chondrogenesis and sex determination.
SOX9 is known to function as a dimer for chondrogenesis gene activation and a monomer for sex determination gene activation.

Purpose of the Study:

To investigate novel DNA binding configurations of the transcription factor SOX9.
To elucidate the mechanism of SOX9-mediated transcriptional activation at the COL9A1 enhancer.

Main Methods:

Identification and analysis of SOX consensus sequences within the COL9A1 collagen gene enhancer.
Functional assays involving site-directed mutagenesis and enhancer activity assessment in chondrocytic and 10T1/2 cells.
Evaluation of SOX9 responsiveness to overexpression via cotransfection experiments.

Main Results:

Four SOX consensus sequences were identified in the COL9A1 enhancer, arranged in two pairs.
Altering spacing between these pairs or mutating individual sites abolished enhancer activity in chondrocytic cells.
SOX9 overexpression activated the enhancer in 10T1/2 cells, with mutations reducing this responsiveness.

Conclusions:

A novel SOX9 transcriptional activation mechanism involves two SOX9 dimers bound to paired sites on the COL9A1 enhancer.
Direct or indirect interaction between these two bound dimers is necessary for functional transcriptional complex formation.
This finding expands the understanding of SOX9's regulatory roles in chondrogenesis.