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Structural investigation of CenP-A containing nucleosomes utilizing single-molecule Förster resonance energy transfer

Author
Sennett, Michael
Published
[University Park, Pennsylvania] : Pennsylvania State University, 2014.
Physical Description
1 electronic document
Additional Creators
Lee, Tae-Hee
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Open Access.
Summary
Interest in how a functional kinetochore assembles at the centromere has grown in recent years as a result of our increased understanding of the chromosome. Centromere Protein A (CenP-A) is a histone H3 variant and is believed to play an essential role in defining the location of the centromere, rather than the DNA sequence. Based on recent crystal structures and models of nucleosomes containing Cenp-A, it has been hypothesized that the structures of Cenp-A nucleosomes is different from that of canonical nucleosomes. , Using single-molecule Förster resonance energy transfer (smFRET), I tested the hypothesis in vitro using physiologically relevant salt conditions. smFRET measurements reveal that the structure of fluorescently labeled DNA in complex with CenP-A containing centromere nucleosomes is different from the canonical nucleosomes. This indicates a specific role for CenP-A variants, suggesting a basis for the mechanism of centromere identification and kinetochore assembly.
Other Subject(s)
Dissertation Note
M.S. Pennsylvania State University 2014.
Technical Details
The full text of the dissertation is available as an Adobe Acrobat .pdf file ; Adobe Acrobat Reader required to view the file.
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