Subtelomere-binding protein Tbf1 and telomere-binding protein Rap1 collaborate to inhibit localization of the Mre11 complex to DNA ends in budding yeast

Fukunaga, Kenzo; Hirano, Yukinori; Sugimoto, Katsunori

doi:10.1091/mbc.e11-06-0568

Cited by 18 publications

(28 citation statements)

References 84 publications

(188 reference statements)

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“…In fission yeast, roles of Taz1 at telomeres are well characterized, whereas the function of Tbf1 is elusive (Cockell et al 2009; Moser and Nakamura 2009). In budding yeast, Tbf1 binds to telomeric repeats localized at subtelomeres, and it has been shown to play a role in telomere homeostasis by suppressing checkpoint activation at short telomeres (Fukunaga et al 2012). Tbf1 is an essential protein in S. pombe due to its function for transcription; however, its role in telomere maintenance in fission yeast is unknown (Cockell et al 2009; Sarda and Hannenhalli 2015; Yan et al 2015).…”

Section: Role Of Swi1–myb/sant Protein Interaction In Dna Replicationmentioning

confidence: 99%

Timeless protection of telomeres

2016

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The DNA replication machinery encounters problems at numerous genomic regions that are inherently difficult to replicate. These genomic regions include telomeres, which contain repetitive DNA and telomere-binding proteins. If not properly regulated, replication of such genomic regions can result in DNA damage, leading to genomic instability. Studies implicated a role of Timeless-related proteins at difficult-to-replicate genomic regions, including telomeres. However, how these proteins maintain telomeres was elusive. In a recent report, we described the role of Swi1, a Timeless-related protein, in telomere maintenance in fission yeast. We demonstrated that Swi1 is required for proper replication of repeat DNA sequences at telomeres. We also showed that Swi1-deficient cells utilize recombination-based ALT (alternative lengthening of telomeres)-like mechanisms to maintain telomeres in the absence of telomerase. Here, we highlight these findings and present additional data to discuss the role of Swi1Timeless in telomere protection and ALT prevention.

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Section: Role Of Swi1–myb/sant Protein Interaction In Dna Replicationmentioning

confidence: 99%

Timeless protection of telomeres

2016

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“…Rif2 inhibits Tel1 binding because both proteins (Sabourin et al 2007) interact with the carboxyl end of Xrs2 and thus compete with each other for MRX association (Hirano et al 2009). Likewise, Tbf1 can inhibit MRX binding to telomeres (Fukunaga et al 2012). In most situations, Tel1 affects only the frequency of telomere lengthening, but at short telomeres it also increases telomerase processivity (Chang et al 2007).…”

Section: Telomerasementioning

confidence: 99%

DNA Repair at Telomeres: Keeping the Ends Intact

Webb

Zakian

2013

Cold Spring Harbor Perspectives in Biology

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The molecular era of telomere biology began with the discovery that telomeres usually consist of G-rich simple repeats and end with 3′ single-stranded tails. Enormous progress has been made in identifying the mechanisms that maintain and replenish telomeric DNA and the proteins that protect them from degradation, fusions, and checkpoint activation. Although telomeres in different organisms (or even in the same organism under different conditions) are maintained by different mechanisms, the disparate processes have the common goals of repairing defects caused by semiconservative replication through G-rich DNA, countering the shortening caused by incomplete replication, and postreplication regeneration of G tails. In addition, standard DNA repair mechanisms must be suppressed or modified at telomeres to prevent their being recognized and processed as DNA double-strand breaks. Here, we discuss the players and processes that maintain and regenerate telomere structure.

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“…This effect can be explained by the fact that Tbf1 and Rap1 cooperate to inhibit accumulation of the MRX complex at DNA ends (Fig. 2A) [73]. Neither the RCT domain of Rap1, nor Rif1 and Rif2, are required for such inhibition, but rather an N‐terminal region of Tbf1.…”

Section: Telomere Length Regulation In S Cerevisiaementioning

confidence: 99%

Telomere length regulation in budding yeasts

Malyavko¹,

Parfenova²,

Zvereva³

et al. 2014

FEBS Letters

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a b s t r a c tTelomeres are the nucleoprotein caps of chromosomes. Their length must be tightly regulated in order to maintain the stability of the genome. This is achieved by the intricate network of interactions between different proteins and protein-RNA complexes. Different organisms use various mechanisms for telomere length homeostasis. However, details of these mechanisms are not yet completely understood. In this review we have summarized our latest achievements in the understanding of telomere length regulation in budding yeasts.

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Subtelomere-binding protein Tbf1 and telomere-binding protein Rap1 collaborate to inhibit localization of the Mre11 complex to DNA ends in budding yeast

Cited by 18 publications

References 84 publications

Timeless protection of telomeres

Timeless protection of telomeres

DNA Repair at Telomeres: Keeping the Ends Intact

Telomere length regulation in budding yeasts

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