The yeast telomerase module for telomere recruitment requires a specific RNA architecture

Laterreur, Nancy; Lemieux, Bruno; Neumann, Hannah; Berger-Dancause, Jean-Christophe; Lafontaine, Daniel A.; Wellinger, Raymund J.

doi:10.1261/rna.066696.118

Cited by 16 publications

(24 citation statements)

References 50 publications

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“…Similar to RNAseP/MRP, where Pop1, 6 and 7 stabilize the RNP structure, telomerase Pop subunits are implicated in stabilization of Est1 and Est2 on TLC1 [25,37]. The Pop-mediated stabilization of telomerase proteins is likely conferred by achieving a precise TLC1 architecture [37]. Introduction of just two base pairs into the short stem between the Est1 and Pop binding sites results in a complete loss of Est1, whereas Pop proteins remained present.…”

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

“…The second stem-loop structure holds the Yku complex [28]. The third arm contains the bulge-stem IVc, which supports Est1 binding at the base [35,36] and the set of Pop proteins at the distal end [25,37].…”

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

“…The Pop proteins are essential for telomerase in vivo function [25]. Similar to RNAseP/MRP, where Pop1, 6 and 7 stabilize the RNP structure, telomerase Pop subunits are implicated in stabilization of Est1 and Est2 on TLC1 [25,37]. The Pop-mediated stabilization of telomerase proteins is likely conferred by achieving a precise TLC1 architecture [37].…”

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

“…In addition, these results show that the Pop complex binds to telomerase in an Est1-independent manner. Altogether, it suggests that both the functional and physical interaction between the Pop complex and Est1 occurs only in the context of the proper TLC1 architecture, which brings the proteins in close proximity to favor their interaction [37]. Whether the Pop complex also interacts with Est3 and affects its stable association with the telomerase complex, is still unknown and will be important to assess.…”

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

“…It is possible that once bound to the telomerase complex, Est3 can be stabilized by other proteins and consequently no longer requires Est2 to keep its position. One of the candidates for such a function is the complex of the Pop1, Pop6 and Pop7 proteins, which might stabilize Est3 binding within the telomerase complex, as they do for Est1 and Est2 [25,37]. In general, although constitutively present in the telomerase RNP, the role of the Pop proteins in telomerase regulation remains unexplored.…”

Section: Regulation Of Telomerase Assembly and Disassembly During Thementioning

confidence: 99%

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Telomerase in Space and Time: Regulation of Yeast Telomerase Function at Telomeres and DNA Breaks

Vasianovich¹,

Krallis²,

Wellinger³

2020

Telomerase and Non-Telomerase Mechanisms of Telomere Maintenance

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A development of new strategies against telomerase-associated disorders, such as dyskeratosis congenita, aplastic anemia or cancer, relies on a detailed understanding of telomerase life cycle and the multiple layers of its regulation. Saccharomyces cerevisiae is a prime model to study telomerase function and it has already revealed many conserved pathways for telomerase biology. In this chapter, we review the current knowledge of the regulatory pathways that control telomerase function in budding yeast. In particular, we discuss the cell cycle-dependent assembly of telomerase and its recruitment to telomeres. We also focus on the mechanisms that target telomerase to short telomeres. Finally, we discuss possible pathways that inhibit telomerase function at DNA double-strand breaks, thus limiting deleterious de novo telomere addition events.

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Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

Section: Interactions Between Telomerase Components Within the Rnp Comentioning

confidence: 99%

Section: Regulation Of Telomerase Assembly and Disassembly During Thementioning

confidence: 99%

See 3 more Smart Citations

Telomerase in Space and Time: Regulation of Yeast Telomerase Function at Telomeres and DNA Breaks

Vasianovich¹,

Krallis²,

Wellinger³

2020

Telomerase and Non-Telomerase Mechanisms of Telomere Maintenance

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Maturation and shuttling of the yeast telomerase RNP: assembling something new using recycled parts

2021

Self Cite

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As the limiting component of the budding yeast telomerase, the Tlc1 RNA must undergo multiple consecutive modifications and rigorous quality checks throughout its lifecycle. These steps will ensure that only correctly processed and matured molecules are assembled into telomerase complexes that subsequently act at telomeres. The complex pathway of Tlc1 RNA maturation, involving 5'- and 3'-end processing, stabilisation and assembly with the protein subunits, requires at least one nucleo-cytoplasmic passage. Furthermore, it appears that the pathway is tightly coordinated with the association of various and changing proteins, including the export factor Xpo1, the Mex67/Mtr2 complex, the Kap122 importin, the Sm7 ring and possibly the CBC and TREX-1 complexes. Although many of these maturation processes also affect other RNA species, the Tlc1 RNA exploits them in a new combination and, therefore, ultimately follows its own and unique pathway. In this review, we highlight recent new insights in maturation and subcellular shuttling of the budding yeast telomerase RNA and discuss how these events may be fine-tuned by the biochemical characteristics of the varying processing and transport factors as well as the final telomerase components. Finally, we indicate outstanding questions that we feel are important to be addressed for a complete understanding of the telomerase RNA lifecycle and that could have implications for the human telomerase as well.

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Methods that shaped telomerase research

Bartle,

Wellinger

2023

Biogerontology

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Telomerase, the ribonucleoprotein (RNP) responsible for telomere maintenance, has a complex life. Complex in that it is made of multiple proteins and an RNA, and complex because it undergoes many changes, and passes through different cell compartments. As such, many methods have been developed to discover telomerase components, delve deep into understanding its structure and function and to figure out how telomerase biology ultimately relates to human health and disease. While some old gold-standard methods are still key for determining telomere length and measuring telomerase activity, new technologies are providing promising new ways to gain detailed information that we have never had access to before. Therefore, we thought it timely to briefly review the methods that have revealed information about the telomerase RNP and outline some of the remaining questions that could be answered using new methodology.

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The yeast telomerase module for telomere recruitment requires a specific RNA architecture

Cited by 16 publications

References 50 publications

Telomerase in Space and Time: Regulation of Yeast Telomerase Function at Telomeres and DNA Breaks

Telomerase in Space and Time: Regulation of Yeast Telomerase Function at Telomeres and DNA Breaks

Maturation and shuttling of the yeast telomerase RNP: assembling something new using recycled parts

Methods that shaped telomerase research

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