How MENT Protein Changes Shape to Help Condense Chromatin
Author Information
Author(s): Ong Poh Chee, Golding Sarah J., Pearce Mary C., Irving James A., Grigoryev Sergei A., Pike Debbie, Langendorf Christopher G., Bashtannyk-Puhalovich Tanya A., Bottomley Stephen P., Whisstock James C., Pike Robert N., McGowan Sheena
Primary Institution: Department of Biochemistry and Molecular Biology, Monash University
Hypothesis
Does the conformational change in MENT depend on the presence of a bound ligand?
Conclusion
MENT undergoes a conformational change in the presence of nucleosomal DNA, which is essential for its role in chromatin condensation.
Supporting Evidence
- MENT is a member of the serpin superfamily and inhibits certain proteases.
- Conformational changes in MENT are essential for its function in chromatin condensation.
- Naked DNA does not induce a conformational change in MENT, but nucleosomal DNA does.
- Mutations in specific regions of MENT affect its ability to undergo conformational changes.
Takeaway
MENT is a protein that helps package DNA in cells, and it changes shape when it binds to certain types of DNA, which helps it do its job better.
Methodology
The study used intrinsic tryptophan fluorescence to measure conformational changes in MENT in the presence of different DNA structures.
Limitations
The study's structural mapping studies were less informative than hoped, limiting the understanding of the precise structural effects of chromatin on MENT.
Digital Object Identifier (DOI)
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