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Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries

The twin-arginine translocase (Tat) pathway transports folded proteins across the plasma membrane and plays a critical role in protein transport in haloarchaea. Computational analysis and previous experimental evidence suggested that the Tat pathway transports almost the entire secretome in haloarch...

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Autores principales: Ghosh, Deepanjan, Boral, Debjyoti, Vankudoth, Koteswara Rao, Ramasamy, Sureshkumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6525301/
https://www.ncbi.nlm.nih.gov/pubmed/31193317
http://dx.doi.org/10.1016/j.heliyon.2019.e01587
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author Ghosh, Deepanjan
Boral, Debjyoti
Vankudoth, Koteswara Rao
Ramasamy, Sureshkumar
author_facet Ghosh, Deepanjan
Boral, Debjyoti
Vankudoth, Koteswara Rao
Ramasamy, Sureshkumar
author_sort Ghosh, Deepanjan
collection PubMed
description The twin-arginine translocase (Tat) pathway transports folded proteins across the plasma membrane and plays a critical role in protein transport in haloarchaea. Computational analysis and previous experimental evidence suggested that the Tat pathway transports almost the entire secretome in haloarchaea. The TatC, receptor component of this pathway shows greater variation in membrane topology in haloarchaea than in other organisms. The presence of a unique fourteen-transmembrane TatC homolog (TatC(t)) in haloarchaea, over and above the expected TatC topological variants, indicates a strong correlation between the additional homologs and the large number of substrates transported via the haloarchaeal Tat pathway. Various combinations of TatC homologs with different topologies—TatC(o), TatC(t), TatC(n), and TatC(x) have been observed in haloarchaea. In this report, on the basis of these combinations we have segregated all haloarchaeal Tat substrates into two groups. The first group consists of substrates that are transported by TatC(t) alone, whereas the second group consists of substrates that are transported by the other TatC homologs (TatC(o), TatC(n), and TatC(x)). The various haloarchaea TatA components also shows the possible segregation towards the substrates. We have also identified the possible homologs for Tat substrate chaperones, which act as a quality-control mechanism for proper protein folding. Further sequence analysis implies that the two TatC domains of TatC(t) complement each other's functionally. Substrate analysis also revealed subtle differences between the substrates being transported by various homologs: further experimental analysis is therefore required for better understanding of the complexities of the haloarchaeal Tat pathway.
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spelling pubmed-65253012019-05-28 Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries Ghosh, Deepanjan Boral, Debjyoti Vankudoth, Koteswara Rao Ramasamy, Sureshkumar Heliyon Article The twin-arginine translocase (Tat) pathway transports folded proteins across the plasma membrane and plays a critical role in protein transport in haloarchaea. Computational analysis and previous experimental evidence suggested that the Tat pathway transports almost the entire secretome in haloarchaea. The TatC, receptor component of this pathway shows greater variation in membrane topology in haloarchaea than in other organisms. The presence of a unique fourteen-transmembrane TatC homolog (TatC(t)) in haloarchaea, over and above the expected TatC topological variants, indicates a strong correlation between the additional homologs and the large number of substrates transported via the haloarchaeal Tat pathway. Various combinations of TatC homologs with different topologies—TatC(o), TatC(t), TatC(n), and TatC(x) have been observed in haloarchaea. In this report, on the basis of these combinations we have segregated all haloarchaeal Tat substrates into two groups. The first group consists of substrates that are transported by TatC(t) alone, whereas the second group consists of substrates that are transported by the other TatC homologs (TatC(o), TatC(n), and TatC(x)). The various haloarchaea TatA components also shows the possible segregation towards the substrates. We have also identified the possible homologs for Tat substrate chaperones, which act as a quality-control mechanism for proper protein folding. Further sequence analysis implies that the two TatC domains of TatC(t) complement each other's functionally. Substrate analysis also revealed subtle differences between the substrates being transported by various homologs: further experimental analysis is therefore required for better understanding of the complexities of the haloarchaeal Tat pathway. Elsevier 2019-05-15 /pmc/articles/PMC6525301/ /pubmed/31193317 http://dx.doi.org/10.1016/j.heliyon.2019.e01587 Text en © 2019 Published by Elsevier Ltd. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Ghosh, Deepanjan
Boral, Debjyoti
Vankudoth, Koteswara Rao
Ramasamy, Sureshkumar
Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
title Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
title_full Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
title_fullStr Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
title_full_unstemmed Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
title_short Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
title_sort analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6525301/
https://www.ncbi.nlm.nih.gov/pubmed/31193317
http://dx.doi.org/10.1016/j.heliyon.2019.e01587
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