The Tenacious Recognition of Yeast Telomere Sequence by Cdc13 is Fully Exerted by a Single OB-fold Domain

Simple item page
dc.contributor.authorLewis, Karen A.
dc.contributor.authorPfaff, Danielle A.
dc.contributor.authorEarley, Jennifer N.
dc.contributor.authorAltschuler, Sarah E.
dc.contributor.authorWuttke, Deborah S.
dc.date.accessioned2020-05-16T18:21:38Z
dc.date.available2020-05-16T18:21:38Z
dc.date.issued2013-09
dc.description.abstractCdc13, the telomere end-binding protein from Saccharomyces cerevisiae, is a multidomain protein that specifically binds telomeric single-stranded DNA (ssDNA) with exquisitely high affinity to coordinate telomere maintenance. Recent structural and genetic data have led to the proposal that Cdc13 is the paralog of RPA70 within a telomere-specific RPA complex. Our understanding of Cdc13 structure and biochemistry has been largely restricted to studies of individual domains, precluding analysis of how each domain influences the activity of the others. To better facilitate a comparison to RPA70, we evaluated the ssDNA binding of full-length S. cerevisiae Cdc13 to its minimal substrate, Tel11. We found that, unlike RPA70 and the other known telomere end-binding proteins, the core Cdc13 ssDNA-binding activity is wholly contained within a single tight-binding oligosaccharide/oligonucleotide/oligopeptide binding (OB)-fold. Because two OB-folds are implicated in dimerization, we also evaluated the relationship between dimerization and ssDNA-binding activity and found that the two activities are independent. We also find that Cdc13 binding exhibits positive cooperativity that is independent of dimerization. This study reveals that, while Cdc13 and RPA70 share similar domain topologies, the corresponding domains have evolved different and specialized functions.
dc.description.departmentChemistry and Biochemistry
dc.formatText
dc.format.extent10 pages
dc.format.medium1 file (.pdf)
dc.identifier.citationLewis, K. A., Pfaff, D. A., Earley, J. N., Altschuler, S. E., & Wuttke, D. S. (2013). The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain. Nucleic Acids Research, 42(1), pp. 475-484.
dc.identifier.doihttps://doi.org/10.1093/nar/gkt843
dc.identifier.issn0305-1048
dc.identifier.urihttps://hdl.handle.net/10877/9942
dc.language.isoen
dc.publisherOxford University Press
dc.rights.holder© 2013 The Author(s).
dc.rights.licenseThis work is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License.
dc.sourceNucleic Acids Research, 2013, Vol. 42, No. 1, pp. 475-484.
dc.subjectyeast telomere sequence
dc.subjectCdc13
dc.subjectOB-fold domain
dc.subjectChemistry and Biochemistry
dc.titleThe Tenacious Recognition of Yeast Telomere Sequence by Cdc13 is Fully Exerted by a Single OB-fold Domain
dc.typeArticle

Files

Original bundle

Now showing 1 - 1 of 1
Thumbnail Image
Name:
gkt843.pdf
Size:
4.52 MB
Format:
Adobe Portable Document Format
Description:
Download

License bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
2.54 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

College of Science and Engineering