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Nuclear Pore-Like Structures in a Compartmentalized Bacterium
Planctomycetes are distinguished from other Bacteria by compartmentalization of cells via internal membranes, interpretation of which has been subject to recent debate regarding potential relations to Gram-negative cell structure. In our interpretation of the available data, the planctomycete Gemmat...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5287468/ https://www.ncbi.nlm.nih.gov/pubmed/28146565 http://dx.doi.org/10.1371/journal.pone.0169432 |
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author | Sagulenko, Evgeny Nouwens, Amanda Webb, Richard I. Green, Kathryn Yee, Benjamin Morgan, Garry Leis, Andrew Lee, Kuo-Chang Butler, Margaret K. Chia, Nicholas Pham, Uyen Thi Phuong Lindgreen, Stinus Catchpole, Ryan Poole, Anthony M. Fuerst, John A. |
author_facet | Sagulenko, Evgeny Nouwens, Amanda Webb, Richard I. Green, Kathryn Yee, Benjamin Morgan, Garry Leis, Andrew Lee, Kuo-Chang Butler, Margaret K. Chia, Nicholas Pham, Uyen Thi Phuong Lindgreen, Stinus Catchpole, Ryan Poole, Anthony M. Fuerst, John A. |
author_sort | Sagulenko, Evgeny |
collection | PubMed |
description | Planctomycetes are distinguished from other Bacteria by compartmentalization of cells via internal membranes, interpretation of which has been subject to recent debate regarding potential relations to Gram-negative cell structure. In our interpretation of the available data, the planctomycete Gemmata obscuriglobus contains a nuclear body compartment, and thus possesses a type of cell organization with parallels to the eukaryote nucleus. Here we show that pore-like structures occur in internal membranes of G.obscuriglobus and that they have elements structurally similar to eukaryote nuclear pores, including a basket, ring-spoke structure, and eight-fold rotational symmetry. Bioinformatic analysis of proteomic data reveals that some of the G. obscuriglobus proteins associated with pore-containing membranes possess structural domains found in eukaryote nuclear pore complexes. Moreover, immunogold labelling demonstrates localization of one such protein, containing a β-propeller domain, specifically to the G. obscuriglobus pore-like structures. Finding bacterial pores within internal cell membranes and with structural similarities to eukaryote nuclear pore complexes raises the dual possibilities of either hitherto undetected homology or stunning evolutionary convergence. |
format | Online Article Text |
id | pubmed-5287468 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-52874682017-02-17 Nuclear Pore-Like Structures in a Compartmentalized Bacterium Sagulenko, Evgeny Nouwens, Amanda Webb, Richard I. Green, Kathryn Yee, Benjamin Morgan, Garry Leis, Andrew Lee, Kuo-Chang Butler, Margaret K. Chia, Nicholas Pham, Uyen Thi Phuong Lindgreen, Stinus Catchpole, Ryan Poole, Anthony M. Fuerst, John A. PLoS One Research Article Planctomycetes are distinguished from other Bacteria by compartmentalization of cells via internal membranes, interpretation of which has been subject to recent debate regarding potential relations to Gram-negative cell structure. In our interpretation of the available data, the planctomycete Gemmata obscuriglobus contains a nuclear body compartment, and thus possesses a type of cell organization with parallels to the eukaryote nucleus. Here we show that pore-like structures occur in internal membranes of G.obscuriglobus and that they have elements structurally similar to eukaryote nuclear pores, including a basket, ring-spoke structure, and eight-fold rotational symmetry. Bioinformatic analysis of proteomic data reveals that some of the G. obscuriglobus proteins associated with pore-containing membranes possess structural domains found in eukaryote nuclear pore complexes. Moreover, immunogold labelling demonstrates localization of one such protein, containing a β-propeller domain, specifically to the G. obscuriglobus pore-like structures. Finding bacterial pores within internal cell membranes and with structural similarities to eukaryote nuclear pore complexes raises the dual possibilities of either hitherto undetected homology or stunning evolutionary convergence. Public Library of Science 2017-02-01 /pmc/articles/PMC5287468/ /pubmed/28146565 http://dx.doi.org/10.1371/journal.pone.0169432 Text en © 2017 Sagulenko et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Sagulenko, Evgeny Nouwens, Amanda Webb, Richard I. Green, Kathryn Yee, Benjamin Morgan, Garry Leis, Andrew Lee, Kuo-Chang Butler, Margaret K. Chia, Nicholas Pham, Uyen Thi Phuong Lindgreen, Stinus Catchpole, Ryan Poole, Anthony M. Fuerst, John A. Nuclear Pore-Like Structures in a Compartmentalized Bacterium |
title | Nuclear Pore-Like Structures in a Compartmentalized Bacterium |
title_full | Nuclear Pore-Like Structures in a Compartmentalized Bacterium |
title_fullStr | Nuclear Pore-Like Structures in a Compartmentalized Bacterium |
title_full_unstemmed | Nuclear Pore-Like Structures in a Compartmentalized Bacterium |
title_short | Nuclear Pore-Like Structures in a Compartmentalized Bacterium |
title_sort | nuclear pore-like structures in a compartmentalized bacterium |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5287468/ https://www.ncbi.nlm.nih.gov/pubmed/28146565 http://dx.doi.org/10.1371/journal.pone.0169432 |
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