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Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein
N Kamata1, R M Jotte, J T Holt
1Department of Cell Biology, Vanderbilt University, Nashville, Tennessee 37232.
Abstract:
FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.
Insights
Protein myristylation of the FBR murine sarcoma virus (gag-Fos) protein reduces its DNA binding and gene transactivation. This modification impacts gene regulation by DNA-binding proteins.
Area of Science:
- Molecular Biology
- Virology
- Gene Regulation
Background:
- Fos proteins are transcription factors crucial for cellular processes.
- Viral oncoproteins can exhibit altered functions compared to their cellular counterparts.
- Post-translational modifications like myristylation can significantly impact protein activity.
Purpose of the Study:
- To investigate the functional differences between virally transduced Fos (gag-Fos) and cellular Fos.
- To determine the role of N-terminal gag region myristylation in gag-Fos activity.
- To elucidate how protein myristylation affects DNA-binding proteins and gene regulation.
Main Methods:
- Biochemical analysis of FBR murine sarcoma virus (gag-Fos) protein.
- Comparison of gene transactivation by gag-Fos and cellular Fos.
- Assessment of DNA binding affinity and Jun protein heterodimerization.
Main Results:
- Virally transduced gag-Fos protein shows reduced gene transactivation compared to cellular Fos.
- Myristylation of the N-terminal gag region of gag-Fos decreases its DNA binding.
- Transcriptional activation is diminished due to myristylation, but Jun protein heterodimerization remains unaffected.
Conclusions:
- Protein myristylation of the gag-Fos oncoprotein impairs its DNA-binding capability.
- Myristylation serves as a regulatory mechanism modulating the gene regulatory function of DNA-binding proteins.
- Understanding these modifications is key to comprehending viral oncogenesis and gene expression control.