Drees, Becky L.’s team published research in Journal of Molecular Biology in 273 | CAS: 70539-42-3

Journal of Molecular Biology published new progress about 70539-42-3. 70539-42-3 belongs to alcohols-buliding-blocks, auxiliary class pyrrolidine,Ester,Amide,Inhibitor,Inhibitor, name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, and the molecular formula is C18H20N2O12, Related Products of alcohols-buliding-blocks.

Drees, Becky L. published the artcileThe GCN4 leucine zipper can functionally substitute for the heat shock transcription factor’s trimerization domain, Related Products of alcohols-buliding-blocks, the publication is Journal of Molecular Biology (1997), 273(1), 61-74, database is CAplus and MEDLINE.

The heat shock transcription factor (HSF) is the only known sequence-specific, homotrimeric DNA-binding protein. HSF binds to a DNA recognition site called a heat shock element (HSE), which contains varying numbers of nGAAn units (“GAA boxes”) arranged in inverted repeats. To investigate the role of trimerization on HSF’s DNA-binding properties, the authors replaced the trimerization domain, which self-assembles to form a three-stranded α-helical coiled coil, with the GCN4 leucine zipper, which forms a two-stranded α-helical coiled coil. Surprisingly, this substitution did not effect the ability of HSF to function in vivo. Biochem. studies of an HSF-leucine zipper chimera in comparison to an HSF truncation show that the HSF-leucine zipper chimera, though dimeric in solution and dimeric when bound to a two-box HSE, forms a trimeric complex when bound to a three-box HSE. The ability to form trimers depends on the presence of three contiguous GAA boxes present in inverted repeats. The proximity of the leucine zippers due to the orientation of the binding sites suggests that the leucine zippers might be forming a three-stranded coiled coil and several experiments lend support to this model. The ability of the leucine zipper to change oligomeric states in context might explain why the leucine zipper can replace the trimerization domain of HSF in vivo.

Journal of Molecular Biology published new progress about 70539-42-3. 70539-42-3 belongs to alcohols-buliding-blocks, auxiliary class pyrrolidine,Ester,Amide,Inhibitor,Inhibitor, name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, and the molecular formula is C18H20N2O12, Related Products of alcohols-buliding-blocks.

Referemce:
https://en.wikipedia.org/wiki/Alcohol,
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