Conserved Structure for Single-Stranded Telomeric DNA Recognition

Mitton-Fry, Rachel M.; Anderson, Emily M.; Hughes, Timothy R.; Lundblad, Victoria; Wuttke, Deborah S.

doi:10.1126/science.1068799

Cited by 168 publications

(202 citation statements)

References 28 publications

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“…* Amino acids that made contact with single-stranded telomeric DNA from NMR analysis [23]. † ADE2-ADE3-based reporter system for plasmid-loss assay (as shown in Figure 1A).…”

Section: Establishing a Genetic Screening Scheme For The Identificatimentioning

confidence: 99%

“…A summary of these mutations is listed in Table 1. Among these mutations, the Tyr 522 , Arg 635 and Ile 633 residues were shown to locate in the DNA-protein interface of Cdc13p [23].…”

Section: Isolation Of Cdc13 Mutants That Lose Cdc13 Essential Functionsmentioning

confidence: 99%

“…Domain mapping studies of Cdc13p have defined telomeric DNA-binding activity to a fragment in the range of amino acids 451-693 [18,22], and further to within amino acids 497-693 [23]. The amino acid region from 190 to 340 is involved in the recruiting of telomerase on to telomeres [24].…”

Section: Introductionmentioning

confidence: 99%

“…We have demonstrated previously [25] that the N-terminal fragment ranging from amino acids 1-251 of Cdc13p interacted with Pol1p, Imp4p, Zds2p and Sir4p and is required for telomere maintenance and cell growth. The structure of the telomeric DNA-binding domain within Cdc13p has been solved [23]. A conserved OB-fold is found in several telomere-binding proteins in other organisms [15,26] [23].…”

Section: Introductionmentioning

confidence: 99%

“…The structure of the telomeric DNA-binding domain within Cdc13p has been solved [23]. A conserved OB-fold is found in several telomere-binding proteins in other organisms [15,26] [23]. Among these residues, mutation of residues Tyr 522 , Ile 633 or Arg 635 severely affects binding activity, suggesting that these residues are important for Cdc13p binding to telomeric DNA [27].…”

Section: Introductionmentioning

confidence: 99%

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Genetic analysis reveals essential and non-essential amino acids within the telomeric DNA-binding interface of Cdc13p

Lin¹,

Lee²,

Lin³

2007

Biochemical Journal

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Cdc13p is a specific single-stranded telomeric DNA-binding protein of Saccharomyces cerevisiae. It is involved in protecting telomeres and regulating telomere length. The telomere-binding domain of Cdc13p is located between residues 497 and 693, and its structure has been resolved by NMR spectroscopy. A series of aromatic, hydrophobic and basic residues located at the DNAbinding surface of Cdc13p are involved in binding to telomeres. Here we applied a genetic approach to analyse the involvements of these residues in telomere binding. A series of mutants within the telomere-binding domain of Cdc13p were identified that failed to complement cdc13 mutants in vivo. Among the amino acids that were isolated, the Tyr 522 , Arg 635 , and Ile 633 residues were shown to locate at the DNA-binding surface. We further demonstrated that Y522C and R635A mutants failed to bind telomeric DNA in vitro, indicating that these residues are indeed required for telomere binding. We did not, however, isolate other mutant residues located at the DNA-binding surface of Cdc13p beyond these three residues. Instead, a mutant on Lys 568 was isolated that did not affect the essential function of Cdc13p. The Lys 568 is also located on the DNA-binding surface of Cdc13p. Thus these results suggested that other DNA-binding residues are not essential for telomere binding. In the present study, we have established a genetic test that enabled the identification of telomere-binding residues of Cdc13p in vivo. This type of analysis provides information on those residues that indeed contribute to telomere binding in vivo.

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“…* Amino acids that made contact with single-stranded telomeric DNA from NMR analysis [23]. † ADE2-ADE3-based reporter system for plasmid-loss assay (as shown in Figure 1A).…”

Section: Establishing a Genetic Screening Scheme For The Identificatimentioning

confidence: 99%

“…A summary of these mutations is listed in Table 1. Among these mutations, the Tyr 522 , Arg 635 and Ile 633 residues were shown to locate in the DNA-protein interface of Cdc13p [23].…”

Section: Isolation Of Cdc13 Mutants That Lose Cdc13 Essential Functionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Genetic analysis reveals essential and non-essential amino acids within the telomeric DNA-binding interface of Cdc13p

Lin¹,

Lee²,

Lin³

2007

Biochemical Journal

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Telomeres in Plant Meiosis: Their Structure, Dynamics and Function

Roberts

Osman

Chris

et al. 2013

Annual Plant Reviews

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Telomeres in Plant Meiosis: Their Structure, Dynamics and Function

Roberts

Osman

Franklin

et al. 2018

Annual Plant Reviews Online

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Although the primary role of the telomeres is to protect the chromosome ends from being recognized and processed as DNA double‐strand breaks, evidence is emerging that they have a pivotal role in early events in the movement and synapsis of homologous chromosomes in the meiotic pathway. Attention has been paid to the bouquet, a nearly universal event, during which the telomeres cluster on the nuclear envelope (NE) in early prophase I. It has been suggested that their close proximity promotes homologous pairing. We have previously shown in wild‐typeArabidopsis thalianathat the telomeres are organized around the nucleolus in somatic cells and during the early stages of meiosis. While still associated with the nucleolus, homologous telomeres undergo pairing at the transition from G2 to leptotene at around the same time as assembly of the axial elements. We do not observe a classical bouquet, but as the homologues synapse during zygotene, the paired telomeres occasionally reveal a loose clustering on the NE, which may represent a transient bouquet. As Arabidopsis homologous telomere pairing precedes transient bouquet formation, we have suggested that close juxtaposition of the homologues by virtue of the tethering of the paired telomeres to the NE may facilitate subsequent chromosome alignment and synapsis. Identifying proteins that link the telomeres and the NE has been stimulated by observations inSchizosaccharomyces pombe, where meiotic telomere clustering at the spindle polar body (SPB) involves Sad1, a SPB protein that is indirectly connected to a telomere binding protein, Rap1. Sad1 and the related protein UNC‐84 fromCaenorhabditis eleganscontain a so‐called SUN domain consisting of conserved C‐terminal protein regions a few hundred amino acids long. SUN domains are usually found following a transmembrane domain and a less conserved region of amino acids. Similar proteins have subsequently been identified in other yeasts and mammalian species. In the mouse and C.elegans, they appear to be required for telomere attachment to the NE and for moving the chromosomes via the telomeres in meiosis. Several components of the NE of plants have only recently been identified. This review focuses on the structure of the telomeres in Arabidopsis and their behaviour in the meiotic pathway. We also discuss recent observations linking a role for the meiotic telomeres and their association with the NE in meiotic prophase I.

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Conserved Structure for Single-Stranded Telomeric DNA Recognition

Cited by 168 publications

References 28 publications

Genetic analysis reveals essential and non-essential amino acids within the telomeric DNA-binding interface of Cdc13p

Genetic analysis reveals essential and non-essential amino acids within the telomeric DNA-binding interface of Cdc13p

Telomeres in Plant Meiosis: Their Structure, Dynamics and Function

Telomeres in Plant Meiosis: Their Structure, Dynamics and Function

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