X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.

Monash University
Dr Ashley Buckle (Managed by)
Viewed: [[ro.stat.viewed]] Cited: [[ro.stat.cited]] Accessed: [[ro.stat.accessed]]
ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=hdl:102.100.100/4&rft.title=X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.&rft.identifier=2H4R&rft.publisher=Monash University&rft.description=&rft.creator=Anonymous& and Cell Biology&rft_subject=Biological Sciences&rft_subject=Medical Biochemistry and Metabolomics&rft_subject=Medical and Health Sciences&rft_subject=Macromolecular Crystallography&rft_subject=Diffraction&rft_subject=Protein Structure&rft_subject=X-Ray&rft_subject=Synchrotron&rft.type=dataset&rft.language=English Go to Data Provider

Contact Information

Monash University


Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages.

User Contributed Tags    

Login to tag this record with meaningful keywords to make it easier to discover