Evolution of CST function in telomere maintenance.
Telomeres consist of an elaborate, higher-order DNA architecture, and a suite of proteins that provide protection for the chromosome terminus by blocking inappropriate recombination and nucleolytic attack. In addition, telomeres facilitate telomeric DNA replication by physical interactions with telomerase and the lagging strand replication machinery. The prevailing view has been that two distinct telomere capping complexes evolved, shelterin in vertebrates and a trimeric complex comprised of Cdc13, Stn1 and Ten1 (CST) in yeast. The recent discovery of a CST-like complex in plants and humans raises new questions about the composition of telomeres and their regulatory mechanisms in multicellular eukaryotes. In this review we discuss the evolving functions and interactions of CST components and their contributions to chromosome end protection and DNA replication.
Price
Carolyn M
CM
Department of Cancer and Cell Biology, University of Cincinnati, Cincinnati, OH, USA. Carolyn.Price@uc.edu
Boltz
Kara A
KA
Chaiken
Mary F
MF
Stewart
Jason A
JA
Beilstein
Mark A
MA
Shippen
Dorothy E
DE
D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry / Q000378:metabolism*; D019143:Evolution, Molecular; D006801:Humans; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D000089804:Shelterin Complex; D016615:Telomere / Q000378:metabolism*; D034501:Telomere-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
C452219:Cdc13 protein, S cerevisiae; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; C544945:Ctc1 protein, human; D029701:Saccharomyces cerevisiae Proteins; D000089804:Shelterin Complex; C428109:Stn1 protein, S cerevisiae; C544946:Stn1 protein, human; C512860:TEN1 protein, S cerevisiae; D034501:Telomere-Binding Proteins