Saccharomyces cerevisiae RAP1 bind to telomeric sequences with spatial flexibility
(2000) In Nucleic Acids Research 28(12). p.2292-2301- Abstract
- A wide divergence has been detected in the telomeric sequences among budding yeast species. Despite their length and homogeneity differences, all these yeast telomeric sequences show a conserved core which closely matches the consensus RAP1-binding sequence. We demonstrate that the RAP1 protein binds this sequence core, without involving the diverged sequences outside the core. in Saccharomyces castellii and Saccharomyces dairensis specific classes of interspersed variant repeats are present. We show here that a RAP1-binding site is formed in these species by connecting two consecutive 8 bp telomeric repeats. DNase I footprint analyses specify the binding site as the 13 bp sequence CTGGGT-GTCTGGG, The RAP1 protein also binds the variant... (More)
- A wide divergence has been detected in the telomeric sequences among budding yeast species. Despite their length and homogeneity differences, all these yeast telomeric sequences show a conserved core which closely matches the consensus RAP1-binding sequence. We demonstrate that the RAP1 protein binds this sequence core, without involving the diverged sequences outside the core. in Saccharomyces castellii and Saccharomyces dairensis specific classes of interspersed variant repeats are present. We show here that a RAP1-binding site is formed in these species by connecting two consecutive 8 bp telomeric repeats. DNase I footprint analyses specify the binding site as the 13 bp sequence CTGGGT-GTCTGGG, The RAP1 protein also binds the variant repeats, although with a lowered affinity. However, a split footprint is produced when RAP1 binds a variant repeat where the two half-sites of the binding site are separated by an additional 6 nt. This is probably caused by the intervening sequence looping out of the RAP1-DNA complex. We suggest that the bipartite subdomain structure of the RAP1 protein allows it to remodel telomeric chromatin, a feature which may be of great relevance for telomeric chromatin assembly and structure in vivo. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4754502
- author
- Cohn, Marita LU and Wahlin, Johan LU
- organization
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nucleic Acids Research
- volume
- 28
- issue
- 12
- pages
- 2292 - 2301
- publisher
- Oxford University Press
- external identifiers
-
- scopus:0034660252
- ISSN
- 1362-4962
- DOI
- 10.1093/nar/28.12.2292
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Genetics (Closed 2011) (011005100)
- id
- c2702eff-e3f0-4493-821f-d54e2b55b65e (old id 4754502)
- date added to LUP
- 2016-04-01 12:02:32
- date last changed
- 2022-02-18 17:06:02
@article{c2702eff-e3f0-4493-821f-d54e2b55b65e, abstract = {{A wide divergence has been detected in the telomeric sequences among budding yeast species. Despite their length and homogeneity differences, all these yeast telomeric sequences show a conserved core which closely matches the consensus RAP1-binding sequence. We demonstrate that the RAP1 protein binds this sequence core, without involving the diverged sequences outside the core. in Saccharomyces castellii and Saccharomyces dairensis specific classes of interspersed variant repeats are present. We show here that a RAP1-binding site is formed in these species by connecting two consecutive 8 bp telomeric repeats. DNase I footprint analyses specify the binding site as the 13 bp sequence CTGGGT-GTCTGGG, The RAP1 protein also binds the variant repeats, although with a lowered affinity. However, a split footprint is produced when RAP1 binds a variant repeat where the two half-sites of the binding site are separated by an additional 6 nt. This is probably caused by the intervening sequence looping out of the RAP1-DNA complex. We suggest that the bipartite subdomain structure of the RAP1 protein allows it to remodel telomeric chromatin, a feature which may be of great relevance for telomeric chromatin assembly and structure in vivo.}}, author = {{Cohn, Marita and Wahlin, Johan}}, issn = {{1362-4962}}, language = {{eng}}, number = {{12}}, pages = {{2292--2301}}, publisher = {{Oxford University Press}}, series = {{Nucleic Acids Research}}, title = {{Saccharomyces cerevisiae RAP1 bind to telomeric sequences with spatial flexibility}}, url = {{http://dx.doi.org/10.1093/nar/28.12.2292}}, doi = {{10.1093/nar/28.12.2292}}, volume = {{28}}, year = {{2000}}, }