Open Access
Journal of Biological Chemistry, volume 288, issue 40, pages 29115-29123
Duplication and Functional Specialization of the Telomere-capping Protein Cdc13 in Candida Species
Publication type: Journal Article
Publication date: 2013-10-01
Journal:
Journal of Biological Chemistry
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 4.8
ISSN: 00219258, 1083351X
PubMed ID:
23965999
Biochemistry
Molecular Biology
Cell Biology
Abstract
Background: Cdc13 in Candida species is small and missing conserved domains. Results: A second Cdc13 homologue (Cdc13B) was shown to form heterodimers with Cdc13 and to mediate overlapping functions in telomere protection. Conclusion: Cdc13 has undergone duplication and functional specialization in a branch of Saccharomycotina yeast. Significance: Understanding the assembly and mechanisms of fungal CST complex provides insights on the evolution and function of this crucial telomere complex. The budding yeast G-tail binding complex CST (Cdc13-Stn1-Ten1) is crucial for both telomere protection and replication. Previous studies revealed a family of Cdc13 orthologues (Cdc13A) in Candida species that are unusually small but are nevertheless responsible for G-tail binding and the regulation of telomere lengths and structures. Here we report the identification and characterization of a second family of Cdc13-like proteins in the Candida clade, named Cdc13B. Phylogenetic analysis and sequence alignment indicate that Cdc13B probably arose through gene duplication prior to Candida speciation. Like Cdc13A, Cdc13B appears to be essential. Deleting one copy each of the CDC13A and CDC13B genes caused a synergistic effect on aberrant telomere elongation and t-circle accumulation, suggesting that the two paralogues mediate overlapping and nonredundant functions in telomere regulation. Interestingly, Cdc13B utilizes its C-terminal OB-fold domain (OB4) to mediate self-association and binding to Cdc13A. Moreover, the stability of the heterodimer is evidently greater than that of either homodimer. Both the Cdc13 A/A homodimer and A/B heterodimer, but not the B/B homodimer, recognized the telomere G-tail repeat with high affinity and sequence specificity. Our results reveal novel evolutionary elaborations of the G-tail-binding protein in Saccharomycotina yeast, suggesting a drastic remodeling of CDC13 that entails gene duplication, fusion, and functional specialization. The repeated and independent duplication of G-tail-binding proteins such as Cdc13 and Pot1 hints at the evolutionary advantage of having multiple G-tail-binding proteins.
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Lue N. F., Chan J. Duplication and Functional Specialization of the Telomere-capping Protein Cdc13 in Candida Species // Journal of Biological Chemistry. 2013. Vol. 288. No. 40. pp. 29115-29123.
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Lue N. F., Chan J. Duplication and Functional Specialization of the Telomere-capping Protein Cdc13 in Candida Species // Journal of Biological Chemistry. 2013. Vol. 288. No. 40. pp. 29115-29123.
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TY - JOUR
DO - 10.1074/jbc.M113.506519
UR - https://doi.org/10.1074%2Fjbc.M113.506519
TI - Duplication and Functional Specialization of the Telomere-capping Protein Cdc13 in Candida Species
T2 - Journal of Biological Chemistry
AU - Lue, Neal F.
AU - Chan, Jamie
PY - 2013
DA - 2013/10/01 00:00:00
PB - American Society for Biochemistry and Molecular Biology
SP - 29115-29123
IS - 40
VL - 288
PMID - 23965999
SN - 0021-9258
SN - 1083-351X
ER -
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@article{2013_Lue,
author = {Neal F. Lue and Jamie Chan},
title = {Duplication and Functional Specialization of the Telomere-capping Protein Cdc13 in Candida Species},
journal = {Journal of Biological Chemistry},
year = {2013},
volume = {288},
publisher = {American Society for Biochemistry and Molecular Biology},
month = {oct},
url = {https://doi.org/10.1074%2Fjbc.M113.506519},
number = {40},
pages = {29115--29123},
doi = {10.1074/jbc.M113.506519}
}
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Lue, Neal F., and Jamie Chan. “Duplication and Functional Specialization of the Telomere-capping Protein Cdc13 in Candida Species.” Journal of Biological Chemistry, vol. 288, no. 40, Oct. 2013, pp. 29115-29123. https://doi.org/10.1074%2Fjbc.M113.506519.