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  DNA-directed assembly of capture tools for constitutional studies of large protein complexes.

Meyer, R., Faesen, A., Vogel, K., Jeganathan, S., Musacchio, A., & Niemeyer, C. M. (2015). DNA-directed assembly of capture tools for constitutional studies of large protein complexes. Small, 11(22), 2669-2674. doi:10.1002/smll.201403544.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C6B0-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C6B4-9
Genre: Journal Article

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 Creators:
Meyer, R., Author
Faesen, A.1, Author              
Vogel, K., Author
Jeganathan, S., Author
Musacchio, A., Author
Niemeyer, C. M., Author
Affiliations:
1Research Group Biochemistry of Signal Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2466695              

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 Abstract: Large supramolecular protein complexes, such as the molecular machinery involved in gene regulation, cell signaling, or cell division, are key in all fundamental processes of life. Detailed elucidation of structure and dynamics of such complexes can be achieved by reverse-engineering parts of the complexes in order to probe their interactions with distinctive binding partners in vitro. The exploitation of DNA nanostructures to mimic partially assembled supramolecular protein complexes in which the presence and state of two or more proteins are decisive for binding of additional building blocks is reported here. To this end, four-way DNA Holliday junction motifs bearing a fluorescein and a biotin tag, for tracking and affinity capture, respectively, are site-specifically functionalized with centromeric protein (CENP) C and CENP-T. The latter serves as baits for binding of the so-called KMN component, thereby mimicking early stages of the assembly of kinetochores, structures that mediate and control the attachment of microtubules to chromosomes in the spindle apparatus. Results from pull-down experiments are consistent with the hypothesis that CENP-C and CENP-T may bind cooperatively to the KMN network.

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Language(s): eng - English
 Dates: 2015-02-032015-06-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/smll.201403544
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Title: Small
Source Genre: Journal
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Pages: - Volume / Issue: 11 (22) Sequence Number: - Start / End Page: 2669 - 2674 Identifier: -