2017
Cheng, W. -H.; Huang, K. -Y.; Huang, P. -J.; Lee, C. -C.; Yeh, Y. -M.; Ku, F. -M.; Lin, R.; Cheng, M. -L.; Chiu, C. -H.; Tang, P.
γ-Carboxymuconolactone decarboxylase: A novel cell cycle-related basal body protein in the early branching eukaryote Trichomonas vaginalis Journal Article
In: Parasites and Vectors, 10 (1), 2017, ISSN: 17563305, (cited By 2).
Abstract | Links | BibTeX | 標籤: Basal Bodies; Benzoates; Carboxy-Lyases; Cell Cycle; Iron; Protozoan Proteins; Trichomonas vaginalis, carboxylyase; gamma carboxymuconolactone decarboxylase; iron; nocodazole; unclassified drug; 4-carboxymuconolactone decarboxylase; benzoic acid derivative; carboxylyase; iron; protozoal protein
@article{Cheng2017,
title = {γ-Carboxymuconolactone decarboxylase: A novel cell cycle-related basal body protein in the early branching eukaryote Trichomonas vaginalis},
author = {W. -H. Cheng and K. -Y. Huang and P. -J. Huang and C. -C. Lee and Y. -M. Yeh and F. -M. Ku and R. Lin and M. -L. Cheng and C. -H. Chiu and P. Tang},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85029884915&doi=10.1186%2fs13071-017-2381-4&partnerID=40&md5=aa319d7d2fc95e9e5fa4b9fdbe3ae817},
doi = {10.1186/s13071-017-2381-4},
issn = {17563305},
year = {2017},
date = {2017-01-01},
journal = {Parasites and Vectors},
volume = {10},
number = {1},
publisher = {BioMed Central Ltd.},
abstract = {Background: γ-Carboxymuconolactone decarboxylase (CMD) participates in the β-ketoadipate pathway, which catalyzes aromatic compounds to produce acetyl- or succinyl-CoA, in prokaryotes and yeast. Our previous study demonstrated that expression of a CMD homologue that contains two signatures (dualCMD) is negatively regulated by iron in Trichomonas vaginalis. However, we were not able to identify the components of the β-ketoadipate pathway in the parasite's genome. These observations prompted us to investigate the biological functions of this novel CMD homologue in T. vaginalis. Methods: The specific anti-TvCMD1 antibody was generated, and the expression of TvCMD1 in T. vaginalis cultured under iron-rich and iron-deficient were evaluated. Phylogenetic, metabolomic and substrate induction (protocatechuate and benzoate) analysis were conducted to clarify the function of dualCMD in trichomonad cells. Subcellular localization of TvCMD1 was observed by confocal microscopy. The cell cycle-related role of TvCMD1 was assessed by treating cells with G2/M inhibitor nocodazole. Results: We confirmed that T. vaginalis is not able to catabolize the aromatic compounds benzoate and protocatechuate, which are known substrates of the β-ketoadipate pathway. Using immunofluorescence microscopy, we found that TvCMD1 is spatially associated with the basal body, a part of the cytoskeletal organizing center in T. vaginalis. TvCMD1 accumulated upon treatment with the G2/M inhibitor nocodazole. Additionally, TvCMD1 was expressed and transported to/from the basal body during cytokinesis, suggesting that TvCMD1 plays a role in cell division. Conclusion: We demonstrated that TvCMD1 is unlikely to participate in the β-ketoadipate pathway and demonstrated that it is a novel basal body-localizing (associated) protein. This model sheds light on the importance of genes that are acquired laterally in the coevolution of ancient protists, which surprisingly functions in cell cycle regulation of T. vaginalis. © 2017 The Author(s).},
note = {cited By 2},
keywords = {Basal Bodies; Benzoates; Carboxy-Lyases; Cell Cycle; Iron; Protozoan Proteins; Trichomonas vaginalis, carboxylyase; gamma carboxymuconolactone decarboxylase; iron; nocodazole; unclassified drug; 4-carboxymuconolactone decarboxylase; benzoic acid derivative; carboxylyase; iron; protozoal protein},
pubstate = {published},
tppubtype = {article}
}
Background: γ-Carboxymuconolactone decarboxylase (CMD) participates in the β-ketoadipate pathway, which catalyzes aromatic compounds to produce acetyl- or succinyl-CoA, in prokaryotes and yeast. Our previous study demonstrated that expression of a CMD homologue that contains two signatures (dualCMD) is negatively regulated by iron in Trichomonas vaginalis. However, we were not able to identify the components of the β-ketoadipate pathway in the parasite's genome. These observations prompted us to investigate the biological functions of this novel CMD homologue in T. vaginalis. Methods: The specific anti-TvCMD1 antibody was generated, and the expression of TvCMD1 in T. vaginalis cultured under iron-rich and iron-deficient were evaluated. Phylogenetic, metabolomic and substrate induction (protocatechuate and benzoate) analysis were conducted to clarify the function of dualCMD in trichomonad cells. Subcellular localization of TvCMD1 was observed by confocal microscopy. The cell cycle-related role of TvCMD1 was assessed by treating cells with G2/M inhibitor nocodazole. Results: We confirmed that T. vaginalis is not able to catabolize the aromatic compounds benzoate and protocatechuate, which are known substrates of the β-ketoadipate pathway. Using immunofluorescence microscopy, we found that TvCMD1 is spatially associated with the basal body, a part of the cytoskeletal organizing center in T. vaginalis. TvCMD1 accumulated upon treatment with the G2/M inhibitor nocodazole. Additionally, TvCMD1 was expressed and transported to/from the basal body during cytokinesis, suggesting that TvCMD1 plays a role in cell division. Conclusion: We demonstrated that TvCMD1 is unlikely to participate in the β-ketoadipate pathway and demonstrated that it is a novel basal body-localizing (associated) protein. This model sheds light on the importance of genes that are acquired laterally in the coevolution of ancient protists, which surprisingly functions in cell cycle regulation of T. vaginalis. © 2017 The Author(s).