NDLI: The Telomere Binding Protein Cdc13 and the Single-Stranded DNA Binding Protein RPA Protect Telomeric DNA from Resection by Exonucleases

Content Provider	PubMed Central
Author	Greetham, Matthew Emmanuel, Skordalakes David, Lydall Connolly, Bernard A.
Copyright Year	2015
Abstract	The telomere is present at the ends of all eukaryotic chromosomes and usually consists of repetitive TG-rich DNA that terminates in a single-stranded 3′ TG extension and a 5′ CA-rich recessed strand. A biochemical assay that allows the in vitro observation of exonuclease-catalyzed degradation (resection) of telomeres has been developed. The approach uses an oligodeoxynucleotide that folds to a stem–loop with a TG-rich double-stranded region and a 3′ single-stranded extension, typical of telomeres. Cdc13, the major component of the telomere-specific CST complex, strongly protects the recessed strand from the 5′ → 3′ exonuclease activity of the model exonuclease from bacteriophage λ. The isolated DNA binding domain of Cdc13 is less effective at shielding telomeres. Protection is specific, not being observed in control DNA lacking the specific TG-rich telomere sequence. RPA, the eukaryotic single-stranded DNA binding protein, also inhibits telomere resection. However, this protein is non-specific, equally hindering the degradation of non-telomere controls.
Related Links	http://dx.doi.org/10.1016/j.jmb.2015.08.002
Ending Page	3030
Page Count	8
Starting Page	3023
File Format	PDF
ISSN	00222836
e-ISSN	10898638
Journal	Journal of Molecular Biology
Issue Number	19
Volume Number	427
Language	English
Publisher	Elsevier
Publisher Date	2015-09-01
Access Restriction	Open
Rights Holder	Elsevier
Subject Keyword	Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology Biophysics

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