Homeodomain protein MHox and MADS protein myocyte enhancer-binding factor-2 converge on a common element in the muscle creatine kinase enhancer
| Autor: | Craig Hinkley, Peter Cserjesi, Brenda Lilly, Eric N. Olson, Michael C. Perry |
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| Rok vydání: | 1994 |
| Předmět: |
Mef2
animal structures Transcription Genetic Molecular Sequence Data Biology Transfection Polymerase Chain Reaction Biochemistry DNA-binding protein Gene Expression Regulation Enzymologic Cell Line Transcription (biology) Enhancer binding Animals Humans Binding site Enhancer Creatine Kinase Molecular Biology Transcription factor Homeodomain Proteins Binding Sites Base Sequence MEF2 Transcription Factors Muscles DNA Cell Biology Molecular biology DNA-Binding Proteins Enhancer Elements Genetic Myogenic Regulatory Factors Mutagenesis embryonic structures Trans-Activators Homeobox Oligonucleotide Probes HeLa Cells Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 269:16740-16745 |
| ISSN: | 0021-9258 |
| Popis: | MHox is a mesoderm-specific homeodomain protein that binds an A/T-rich element that is essential for activity of the muscle creatine kinase (MCK) enhancer. The MHox binding site also binds the ubiquitous homeodomain protein Oct-1 as well as myocyte enhancer-binding factor-2 (MEF2), which belongs to the MADS superfamily of transactivators. To determine which of these proteins activates MCK transcription through the A/T element, we mutated this sequence such that it would selectively bind MHox, MEF2, or Oct-1 and tested the activities of the mutant enhancers in skeletal muscle cells. These mutant enhancers revealed that only MEF2 is able to activate the MCK enhancer through the A/T element. The convergence of homeodomain and MADS proteins on the A/T element in the MCK enhancer provides a mechanism through which a single DNA sequence can mediate positive and negative regulation of gene transcription and is reminiscent of the roles of these two classes of transcription factors in the control of other cell-specific genes. |
| Databáze: | OpenAIRE |
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