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Structure and function of the telomeric CST complex

Telomeres comprise the ends of eukaryotic chromosomes and are essential for cell proliferation and genome maintenance. Telomeres are replicated by telomerase, a ribonucleoprotein (RNP) reverse transcriptase, and are maintained primarily by nucleoprotein complexes such as shelterin (TRF1, TRF2, TIN2,...

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Detalles Bibliográficos
Autores principales: Rice, Cory, Skordalakes, Emmanuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4872678/
https://www.ncbi.nlm.nih.gov/pubmed/27239262
http://dx.doi.org/10.1016/j.csbj.2016.04.002
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author Rice, Cory
Skordalakes, Emmanuel
author_facet Rice, Cory
Skordalakes, Emmanuel
author_sort Rice, Cory
collection PubMed
description Telomeres comprise the ends of eukaryotic chromosomes and are essential for cell proliferation and genome maintenance. Telomeres are replicated by telomerase, a ribonucleoprotein (RNP) reverse transcriptase, and are maintained primarily by nucleoprotein complexes such as shelterin (TRF1, TRF2, TIN2, RAP1, POT1, TPP1) and CST (Cdc13/Ctc1, Stn1, Ten1). The focus of this review is on the CST complex and its role in telomere maintenance. Although initially thought to be unique to yeast, it is now evident that the CST complex is present in a diverse range of organisms where it contributes to genome maintenance. The CST accomplishes these tasks via telomere capping and by regulating telomerase and DNA polymerase alpha-primase (polα-primase) access to telomeres, a process closely coordinated with the shelterin complex in most organisms. The goal of this review is to provide a brief but comprehensive account of the diverse, and in some cases organism-dependent, functions of the CST complex and how it contributes to telomere maintenance and cell proliferation.
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spelling pubmed-48726782016-05-27 Structure and function of the telomeric CST complex Rice, Cory Skordalakes, Emmanuel Comput Struct Biotechnol J Short Survey Telomeres comprise the ends of eukaryotic chromosomes and are essential for cell proliferation and genome maintenance. Telomeres are replicated by telomerase, a ribonucleoprotein (RNP) reverse transcriptase, and are maintained primarily by nucleoprotein complexes such as shelterin (TRF1, TRF2, TIN2, RAP1, POT1, TPP1) and CST (Cdc13/Ctc1, Stn1, Ten1). The focus of this review is on the CST complex and its role in telomere maintenance. Although initially thought to be unique to yeast, it is now evident that the CST complex is present in a diverse range of organisms where it contributes to genome maintenance. The CST accomplishes these tasks via telomere capping and by regulating telomerase and DNA polymerase alpha-primase (polα-primase) access to telomeres, a process closely coordinated with the shelterin complex in most organisms. The goal of this review is to provide a brief but comprehensive account of the diverse, and in some cases organism-dependent, functions of the CST complex and how it contributes to telomere maintenance and cell proliferation. Research Network of Computational and Structural Biotechnology 2016-04-14 /pmc/articles/PMC4872678/ /pubmed/27239262 http://dx.doi.org/10.1016/j.csbj.2016.04.002 Text en © 2016 Natrix Separations http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Short Survey
Rice, Cory
Skordalakes, Emmanuel
Structure and function of the telomeric CST complex
title Structure and function of the telomeric CST complex
title_full Structure and function of the telomeric CST complex
title_fullStr Structure and function of the telomeric CST complex
title_full_unstemmed Structure and function of the telomeric CST complex
title_short Structure and function of the telomeric CST complex
title_sort structure and function of the telomeric cst complex
topic Short Survey
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4872678/
https://www.ncbi.nlm.nih.gov/pubmed/27239262
http://dx.doi.org/10.1016/j.csbj.2016.04.002
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