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Telomerase structures and regulation: shedding light on the chromosome end.

ABSTRACT: During genome replication, telomerase adds repeats to the ends of chromosomes to balance the loss of telomeric DNA. The regulation of telomerase activity is of medical relevance, as it has been implicated in human diseases such as cancer, as well as in aging. Until recently, structural information on this enzyme that would facilitate its clinical manipulation had been lacking due to telomerase very low abundance in cells. Recent cryo-EM structures of both the human and Tetrahymena thermophila telomerases have provided a picture of both the shared catalytic core of telomerase and its interaction with species-specific factors that play different roles in telomerase RNP assembly and function. We discuss also progress toward an understanding of telomerase RNP biogenesis and telomere recruitment from recent studies.

SUBMITTER: Nguyen THD

PROVIDER: S-EPMC8240480 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Telomerase structures and regulation: shedding light on the chromosome end.

Nguyen Thi Hoang Duong THD Collins Kathleen K Nogales Eva E

Current opinion in structural biology 20190401

During genome replication, telomerase adds repeats to the ends of chromosomes to balance the loss of telomeric DNA. The regulation of telomerase activity is of medical relevance, as it has been implicated in human diseases such as cancer, as well as in aging. Until recently, structural information on this enzyme that would facilitate its clinical manipulation had been lacking due to telomerase very low abundance in cells. Recent cryo-EM structures of both the human and Tetrahymena thermophila te ...[more]

PMID: 31202023

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Project description:This article explores the important, and yet often overlooked, solid-state structures of selected bioaromatic compounds commonly found in lignin hydrogenolysis oil, a renewable bio-oil that holds great promise to substitute fossil-based aromatic molecules in a wide range of chemical and material industrial applications. At first, single-crystal X-ray diffraction (SCXRD) was applied to the lignin model compounds, dihydroconiferyl alcohol, propyl guaiacol, and eugenol dimers, in order to elucidate the fundamental molecular interactions present in such small lignin-derived polyols. Then, considering the potential use of these lignin-derived molecules as building blocks for polymer applications, structural analysis was also performed for two chemically modified model compounds, i.e., the methylene-bridging propyl-guaiacol dimer and propyl guaiacol and eugenol glycidyl ethers, which can be used as precursors in phenolic and epoxy resins, respectively, thus providing additional information on how the molecular packing is altered following chemical modifications. In addition to the expected H-bonding interactions, other interactions such as π-π stacking and C-H∙∙∙π were observed. This resulted in unexpected trends in the tendencies towards the crystallization of lignin compounds. This was further explored with the aid of DSC analysis and CLP intermolecular energy calculations, where the relationship between the major interactions observed in all the SCXRD solid-state structures and their physico-chemical properties were evaluated alongside other non-crystallizable lignin model compounds. Beyond lignin model compounds, our findings could also provide important insights into the solid-state structure and the molecular organization of more complex lignin fragments, paving the way to the more efficient design of lignin-based materials with improved properties for industrial applications or improving downstream processing of lignin oils in biorefining processes, such as in enhancing the separation and isolation of specific bioaromatic compounds).

Dataset Information

Telomerase structures and regulation: shedding light on the chromosome end.

Publications

Telomerase structures and regulation: shedding light on the chromosome end.

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