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Cellular origin of the viral capsid-like bacterial microcompartments
ᅟ: Bacterial microcompartments (BMC) are proteinaceous organelles that structurally resemble viral capsids, but encapsulate enzymes that perform various specialized biochemical reactions in the cell cytoplasm. The BMC are constructed from two major shell proteins, BMC-H and BMC-P, which form the fac...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5683377/ https://www.ncbi.nlm.nih.gov/pubmed/29132422 http://dx.doi.org/10.1186/s13062-017-0197-y |
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author | Krupovic, Mart Koonin, Eugene V. |
author_facet | Krupovic, Mart Koonin, Eugene V. |
author_sort | Krupovic, Mart |
collection | PubMed |
description | ᅟ: Bacterial microcompartments (BMC) are proteinaceous organelles that structurally resemble viral capsids, but encapsulate enzymes that perform various specialized biochemical reactions in the cell cytoplasm. The BMC are constructed from two major shell proteins, BMC-H and BMC-P, which form the facets and vertices of the icosahedral assembly, and are functionally equivalent to the major and minor capsid proteins of viruses, respectively. This equivalence notwithstanding, neither of the BMC proteins displays structural similarity to known capsid proteins, rendering the origins of the BMC enigmatic. Here, using structural and sequence comparisons, we show that both BMC-H and BMC-P, most likely, were exapted from bona fide cellular proteins, namely, PII signaling protein and OB-fold domain-containing protein, respectively. This finding is in line with the hypothesis that many major viral structural proteins have been recruited from cellular proteomes. REVIEWERS: This article was reviewed by Igor Zhulin, Jeremy Selengut and Narayanaswamy Srinivasan. For complete reviews, see the Reviewers’ reports section. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13062-017-0197-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5683377 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-56833772017-11-20 Cellular origin of the viral capsid-like bacterial microcompartments Krupovic, Mart Koonin, Eugene V. Biol Direct Discovery Notes ᅟ: Bacterial microcompartments (BMC) are proteinaceous organelles that structurally resemble viral capsids, but encapsulate enzymes that perform various specialized biochemical reactions in the cell cytoplasm. The BMC are constructed from two major shell proteins, BMC-H and BMC-P, which form the facets and vertices of the icosahedral assembly, and are functionally equivalent to the major and minor capsid proteins of viruses, respectively. This equivalence notwithstanding, neither of the BMC proteins displays structural similarity to known capsid proteins, rendering the origins of the BMC enigmatic. Here, using structural and sequence comparisons, we show that both BMC-H and BMC-P, most likely, were exapted from bona fide cellular proteins, namely, PII signaling protein and OB-fold domain-containing protein, respectively. This finding is in line with the hypothesis that many major viral structural proteins have been recruited from cellular proteomes. REVIEWERS: This article was reviewed by Igor Zhulin, Jeremy Selengut and Narayanaswamy Srinivasan. For complete reviews, see the Reviewers’ reports section. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13062-017-0197-y) contains supplementary material, which is available to authorized users. BioMed Central 2017-11-13 /pmc/articles/PMC5683377/ /pubmed/29132422 http://dx.doi.org/10.1186/s13062-017-0197-y Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Discovery Notes Krupovic, Mart Koonin, Eugene V. Cellular origin of the viral capsid-like bacterial microcompartments |
title | Cellular origin of the viral capsid-like bacterial microcompartments |
title_full | Cellular origin of the viral capsid-like bacterial microcompartments |
title_fullStr | Cellular origin of the viral capsid-like bacterial microcompartments |
title_full_unstemmed | Cellular origin of the viral capsid-like bacterial microcompartments |
title_short | Cellular origin of the viral capsid-like bacterial microcompartments |
title_sort | cellular origin of the viral capsid-like bacterial microcompartments |
topic | Discovery Notes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5683377/ https://www.ncbi.nlm.nih.gov/pubmed/29132422 http://dx.doi.org/10.1186/s13062-017-0197-y |
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