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Highly sequence-specific binding is retained within the DNA-binding domain of the Saccharomyces castellii Cdc13 telomere-binding protein

Rhodin, Jenny LU ; Tati, Ramesh LU and Cohn, Marita LU (2008) In FEMS Yeast Research 8(8). p.1289-1302
Abstract
The essential protein Cdc13p binds the single-stranded telomeric 3' overhangs in Saccharomyces cerevisiae and takes part in the regulation of telomere length. The DNA-binding domain (DBD) of Cdc13p is structurally established by an oligonucleotide/oligosaccharide-binding (OB)-fold domain. The sequence homolog in Saccharomyces castellii (scasCDC13) was characterized previously, and the full-length protein was found to bind telomeric DNA specifically. Here, the DBD of scasCdc13p was defined to the central part (402-658) of the protein. The region necessary for forming the scasCdc13p-DBD is larger than the minimal DBD of S. cerevisiae Cdc13p. Deletion of this extended DBD region from the full-length protein completely abolished the DNA... (More)
The essential protein Cdc13p binds the single-stranded telomeric 3' overhangs in Saccharomyces cerevisiae and takes part in the regulation of telomere length. The DNA-binding domain (DBD) of Cdc13p is structurally established by an oligonucleotide/oligosaccharide-binding (OB)-fold domain. The sequence homolog in Saccharomyces castellii (scasCDC13) was characterized previously, and the full-length protein was found to bind telomeric DNA specifically. Here, the DBD of scasCdc13p was defined to the central part (402-658) of the protein. The region necessary for forming the scasCdc13p-DBD is larger than the minimal DBD of S. cerevisiae Cdc13p. Deletion of this extended DBD region from the full-length protein completely abolished the DNA binding, indicating the importance of the extended region for the correct formation of a binding-competent DBD. The scasCdc13p-DBD bound the same 8-mer minimal binding site as the full-length protein, but an extension of the target site in the 3' end increased the stability of the DNA-protein complex. Significantly, scasCdc13p-DBD showed a retained high sequence specific binding, where the four nucleotides of most importance for the sequence specificity are highly conserved in eukaryotic telomeric repeats. Thus, the unique single-stranded DNA-binding properties of the full-length protein are entirely retained within the isolated scasCdc13p-DBD. (Less)
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
DNA-binding protein, Saccharomyces castellii, telomere, CDC13, single-stranded overhang
in
FEMS Yeast Research
volume
8
issue
8
pages
1289 - 1302
publisher
Oxford University Press
external identifiers
  • wos:000260537300009
  • scopus:55349104516
ISSN
1567-1364
DOI
10.1111/j.1567-1364.2008.00431.x
language
English
LU publication?
yes
id
60c3547e-02f0-44f0-b227-86fb3ef59405 (old id 1283923)
date added to LUP
2016-04-01 12:19:42
date last changed
2022-03-21 02:39:20
@article{60c3547e-02f0-44f0-b227-86fb3ef59405,
  abstract     = {{The essential protein Cdc13p binds the single-stranded telomeric 3' overhangs in Saccharomyces cerevisiae and takes part in the regulation of telomere length. The DNA-binding domain (DBD) of Cdc13p is structurally established by an oligonucleotide/oligosaccharide-binding (OB)-fold domain. The sequence homolog in Saccharomyces castellii (scasCDC13) was characterized previously, and the full-length protein was found to bind telomeric DNA specifically. Here, the DBD of scasCdc13p was defined to the central part (402-658) of the protein. The region necessary for forming the scasCdc13p-DBD is larger than the minimal DBD of S. cerevisiae Cdc13p. Deletion of this extended DBD region from the full-length protein completely abolished the DNA binding, indicating the importance of the extended region for the correct formation of a binding-competent DBD. The scasCdc13p-DBD bound the same 8-mer minimal binding site as the full-length protein, but an extension of the target site in the 3' end increased the stability of the DNA-protein complex. Significantly, scasCdc13p-DBD showed a retained high sequence specific binding, where the four nucleotides of most importance for the sequence specificity are highly conserved in eukaryotic telomeric repeats. Thus, the unique single-stranded DNA-binding properties of the full-length protein are entirely retained within the isolated scasCdc13p-DBD.}},
  author       = {{Rhodin, Jenny and Tati, Ramesh and Cohn, Marita}},
  issn         = {{1567-1364}},
  keywords     = {{DNA-binding protein; Saccharomyces castellii; telomere; CDC13; single-stranded overhang}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{1289--1302}},
  publisher    = {{Oxford University Press}},
  series       = {{FEMS Yeast Research}},
  title        = {{Highly sequence-specific binding is retained within the DNA-binding domain of the Saccharomyces castellii Cdc13 telomere-binding protein}},
  url          = {{http://dx.doi.org/10.1111/j.1567-1364.2008.00431.x}},
  doi          = {{10.1111/j.1567-1364.2008.00431.x}},
  volume       = {{8}},
  year         = {{2008}},
}