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Characterization of the DNA binding features of Saccharomyces castellii Cdc13p

Rhodin, Jenny LU ; Astromskas, Eimantas LU and Cohn, Marita LU (2006) In Journal of Molecular Biology 355(3). p.335-346
Abstract
The principal function of Saccharomyces cerevisiae Cdc13p is to provide a loading platform to recruit complexes that provide end protection and telomere replication. We isolated the Saccharomyces castellii Cdc13p homolog (scasCdc13p) and characterized the in vitro DNA binding features of the purified recombinant scasCdc13p. The full-length scasCdc13p binds specifically to G-rich single-stranded telomeric DNA, and not to double-stranded DNA or the C-rich strand. Moreover, the minimal binding site for scasCdc13p is the octamer 5'-GTGTCTGG-3' of the S. castellii telomeric sequence. The scasCdc13p displayed a high affinity binding, where four individual nucleotide residues were found to be of most importance for the sequence specificity.... (More)
The principal function of Saccharomyces cerevisiae Cdc13p is to provide a loading platform to recruit complexes that provide end protection and telomere replication. We isolated the Saccharomyces castellii Cdc13p homolog (scasCdc13p) and characterized the in vitro DNA binding features of the purified recombinant scasCdc13p. The full-length scasCdc13p binds specifically to G-rich single-stranded telomeric DNA, and not to double-stranded DNA or the C-rich strand. Moreover, the minimal binding site for scasCdc13p is the octamer 5'-GTGTCTGG-3' of the S. castellii telomeric sequence. The scasCdc13p displayed a high affinity binding, where four individual nucleotide residues were found to be of most importance for the sequence specificity. Nonetheless, scasCdc13p binds the telomeric repeats from various other species, including the human. In spite of considerable divergence in telomere repeat length and sequence between these species, a conserved Cdc13p binding motif was detected. Among the budding yeasts this conserved Cdc13p binding site overlaps the Rap1p binding site. Together, these data implicate scasCdc13p as a telomere end-binding protein with a potential role in the regulation of telomere maintenance in vivo. Moreover, the results suggest that Rap 1p and Cdc13p act together to preserve the conserved core present within the otherwise highly divergent btelomeric sequences among a wide variety of yeasts. (Less)
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
telomere, DNA-binding protein, single-strand DNA, CDC13, S. castellii
in
Journal of Molecular Biology
volume
355
issue
3
pages
335 - 346
publisher
Elsevier
external identifiers
  • wos:000234609600002
  • pmid:16318854
  • scopus:28944434893
ISSN
1089-8638
DOI
10.1016/j.jmb.2005.10.078
language
English
LU publication?
yes
id
a6d8fc1c-3e35-4f86-94c3-8c1312ca1afd (old id 421289)
date added to LUP
2016-04-01 16:55:42
date last changed
2021-08-11 03:50:37
@article{a6d8fc1c-3e35-4f86-94c3-8c1312ca1afd,
  abstract     = {The principal function of Saccharomyces cerevisiae Cdc13p is to provide a loading platform to recruit complexes that provide end protection and telomere replication. We isolated the Saccharomyces castellii Cdc13p homolog (scasCdc13p) and characterized the in vitro DNA binding features of the purified recombinant scasCdc13p. The full-length scasCdc13p binds specifically to G-rich single-stranded telomeric DNA, and not to double-stranded DNA or the C-rich strand. Moreover, the minimal binding site for scasCdc13p is the octamer 5'-GTGTCTGG-3' of the S. castellii telomeric sequence. The scasCdc13p displayed a high affinity binding, where four individual nucleotide residues were found to be of most importance for the sequence specificity. Nonetheless, scasCdc13p binds the telomeric repeats from various other species, including the human. In spite of considerable divergence in telomere repeat length and sequence between these species, a conserved Cdc13p binding motif was detected. Among the budding yeasts this conserved Cdc13p binding site overlaps the Rap1p binding site. Together, these data implicate scasCdc13p as a telomere end-binding protein with a potential role in the regulation of telomere maintenance in vivo. Moreover, the results suggest that Rap 1p and Cdc13p act together to preserve the conserved core present within the otherwise highly divergent btelomeric sequences among a wide variety of yeasts.},
  author       = {Rhodin, Jenny and Astromskas, Eimantas and Cohn, Marita},
  issn         = {1089-8638},
  language     = {eng},
  number       = {3},
  pages        = {335--346},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Biology},
  title        = {Characterization of the DNA binding features of Saccharomyces castellii Cdc13p},
  url          = {http://dx.doi.org/10.1016/j.jmb.2005.10.078},
  doi          = {10.1016/j.jmb.2005.10.078},
  volume       = {355},
  year         = {2006},
}