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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...

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Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
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.
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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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