Dynamic DNA Shortening by Telomere-Binding Protein Cdc13

2021 ◽  
Author(s):  
Yi-Yun Lin ◽  
Min-Hsuan Li ◽  
Yen-Chan Chang ◽  
Peng-Yu Fu ◽  
Ryosuke L. Ohniwa ◽  
...  
Keyword(s):  
Binding Protein ◽  
Telomere Binding Protein

Association of the telomere-telomere-binding protein complex of hypotrichous ciliates with the nuclear matrix and dissociation during replication

2001 ◽  
Vol 114 (10) ◽  
pp. 1861-1866 ◽  
Author(s):  
J. Postberg ◽  
S.A. Juranek ◽  
S. Feiler ◽  
H. Kortwig ◽  
F. Jonsson ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Nuclear Localization ◽  
Nuclear Matrix ◽  
Binding Protein ◽  
Specific Interaction ◽  
Eukaryotic Cells ◽  
Dna Molecules ◽  
Telomere Binding Protein ◽  
The Matrix

Telomeric interactions with the nuclear matrix have been described in a variety of eukaryotic cells and seem to be essential for specific nuclear localization. Macronuclear DNA of hypotrichous ciliates occurs in small gene-sized DNA molecules, each being terminated by telomeres. Each macronucleus contains over 10(8)individual DNA molecules. Owing to the high number of telomeres present in this nucleus it provides an excellent model to study telomere behaviour throughout the cell cycle. In this study we provide experimental evidence that the telomere-telomere-binding protein (TEBP) complex specifically interacts with components of the nuclear matrix in vivo. In the course of replication the specific interaction of the TEBP with components of the nuclear matrix is resolved and an attachment of the telomeres to the matrix no longer occurs.

scholarly journals The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase α and the telomerase-associated Est1 protein

2000 ◽  
Vol 14 (14) ◽  
pp. 1777-1788 ◽  
Author(s):  
Haiyan Qi ◽  
Virginia A. Zakian
Keyword(s):  
Dna Polymerase ◽  
Binding Protein ◽  
Point Mutations ◽  
Single Strand ◽  
Catalytic Subunit ◽  
Full Length ◽  
Temperature Sensitive ◽  
Dna Polymerase Α ◽  
Telomere Binding Protein

Saccharomyces telomeres consist of ∼350 bp of C1-3A/TG1-3 DNA. Most of this ∼350 bp is replicated by standard, semiconservative DNA replication. After conventional replication, the C1-3A strand is degraded to generate a long single strand TG1-3 tail that can serve as a substrate for telomerase. Cdc13p is a single strand TG1-3DNA-binding protein that localizes to telomeres in vivo. Genetic data suggest that the Cdc13p has multiple roles in telomere replication. We used two hybrid analysis to demonstrate that Cdc13p interacted with both the catalytic subunit of DNA polymerase α, Pol1p, and the telomerase RNA-associated protein, Est1p. The association of these proteins was confirmed by biochemical analysis using full-length or nearly full-length proteins. Point mutations in either CDC13 orPOL1 that reduced the Cdc13p–Pol1p interaction resulted in telomerase mediated telomere lengthening. Over–expression of the carboxyl terminus of Est1p partially suppressed the temperature sensitive lethality of a cdc13-1 strain. We propose that Cdc13p's interaction with Est1p promotes TG1-3 strand lengthening by telomerase and its interaction with Pol1p promotes C1-3A strand resynthesis by DNA polymerase α.

scholarly journals The C Terminus of the Major Yeast Telomere Binding Protein Rap1p Enhances Telomere Formation

1998 ◽  
Vol 18 (3) ◽  
pp. 1284-1295 ◽  
Author(s):  
Alo Ray ◽  
Kurt W. Runge
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Reverse Transcriptase ◽  
Binding Site ◽  
Binding Protein ◽  
Telomerase Activity ◽  
Telomerase Rna ◽  
Constant Length ◽  
C Terminus ◽  
Telomere Binding Protein ◽  
Yeast Telomere

ABSTRACT The telomeres of most organisms consist of short repeated sequences that can be elongated by telomerase, a reverse transcriptase complex that contains its own RNA template for the synthesis of telomere repeats. In Saccharomyces cerevisiae, the RAP1gene encodes the major telomere binding protein Rap1p. Here we use a quantitative telomere formation assay to demonstrate that Rap1p C termini can enhance telomere formation more than 30-fold when they are located at internal sites. This stimulation is distinct from protection from degradation. Enhancement of formation required the gene for telomerase RNA but not Sir1p, Sir2p, Sir3p, Sir4p, Tel1p, or the Rif1p binding site in the Rap1p C terminus. Our data suggest that Rap1p C termini enhance telomere formation by attracting or increasing the activity of telomerase near telomeres. Earlier work suggests that Rap1p molecules at the chromosome terminus inhibit the elongation of long telomeres by blocking the access of telomerase. Our results suggest a model where a balance between internal Rap1p increasing telomerase activity and Rap1p at the termini of long telomeres controlling telomerase access maintains telomeres at a constant length.

scholarly journals Fission yeast telomere-binding protein Taz1 is a functional but not a structural counterpart of human TRF1 and TRF2

Cell Research ◽  
2015 ◽  
Vol 25 (7) ◽  
pp. 881-884 ◽  
Author(s):  
Wei Deng ◽  
Jian Wu ◽  
Feng Wang ◽  
Junko Kanoh ◽  
Pierre-Marie Dehe ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Binding Protein ◽  
Telomere Binding Protein ◽  
Yeast Telomere

scholarly journals Fission Yeast Taz1 and RPA Are Synergistically Required to Prevent Rapid Telomere Loss

2007 ◽  
Vol 18 (6) ◽  
pp. 2378-2387 ◽  
Author(s):  
Tatsuya Kibe ◽  
Yuuki Ono ◽  
Koichiro Sato ◽  
Masaru Ueno
Keyword(s):  
Fission Yeast ◽  
Binding Protein ◽  
Protein A ◽  
Telomere Maintenance ◽  
Helicase Domain ◽  
Recq Helicase ◽  
Telomeric Dna ◽  
Telomere Binding Protein ◽  
Recombination Repair ◽  
Telomere Loss

The telomere complex must allow nucleases and helicases to process chromosome ends to make them substrates for telomerase, while preventing these same activities from disrupting chromosome end-protection. Replication protein A (RPA) binds to single-stranded DNA and is required for DNA replication, recombination, repair, and telomere maintenance. In fission yeast, the telomere binding protein Taz1 protects telomeres and negatively regulates telomerase. Here, we show that taz1-d rad11-D223Y double mutants lose their telomeric DNA, indicating that RPA (Rad11) and Taz1 are synergistically required to prevent telomere loss. Telomere loss in the taz1-d rad11-D223Y double mutants was suppressed by additional mutation of the helicase domain in a RecQ helicase (Rqh1), or by overexpression of Pot1, a single-strand telomere binding protein that is essential for protection of chromosome ends. From our results, we propose that in the absence of Taz1 and functional RPA, Pot1 cannot function properly and the helicase activity of Rqh1 promotes telomere loss. Our results suggest that controlling the activity of Rqh1 at telomeres is critical for the prevention of genomic instability.

Evolution of the scrambled germline gene encoding α-telomere binding protein in three hypotrichous ciliates

Chromosoma ◽  
1998 ◽  
Vol 107 (5) ◽  
pp. 293-303 ◽  
Author(s):  
Jason D. Prescott ◽  
Michelle L. DuBois ◽  
David M. Prescott
Keyword(s):  
Binding Protein ◽  
Germline Gene ◽  
Gene Encoding ◽  
Telomere Binding Protein

scholarly journals The Protein hSnm1B Is Stabilized When Bound to the Telomere-binding Protein TRF2

2008 ◽  
Vol 283 (35) ◽  
pp. 23671-23676 ◽  
Author(s):  
Brian D. Freibaum ◽  
Christopher M. Counter
Keyword(s):  
Binding Protein ◽  
Telomere Binding Protein
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