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The pupylation pathway and its role in mycobacteria
Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is conjugated to lysine residues of proteins, marking them for proteasomal degradation. Although functionally related...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3511204/ https://www.ncbi.nlm.nih.gov/pubmed/23198822 http://dx.doi.org/10.1186/1741-7007-10-95 |
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author | Barandun, Jonas Delley, Cyrille L Weber-Ban, Eilika |
author_facet | Barandun, Jonas Delley, Cyrille L Weber-Ban, Eilika |
author_sort | Barandun, Jonas |
collection | PubMed |
description | Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is conjugated to lysine residues of proteins, marking them for proteasomal degradation. Although functionally related to ubiquitination, pupylation is carried out by different enzymes that are evolutionarily linked to bacterial carboxylate-amine ligases. Here, we compare the mechanism of Pup-conjugation to target proteins with ubiquitination, describe the evolutionary emergence of pupylation and discuss the importance of this pathway for survival of Mycobacterium tuberculosis in the host. |
format | Online Article Text |
id | pubmed-3511204 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-35112042012-12-01 The pupylation pathway and its role in mycobacteria Barandun, Jonas Delley, Cyrille L Weber-Ban, Eilika BMC Biol Review Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is conjugated to lysine residues of proteins, marking them for proteasomal degradation. Although functionally related to ubiquitination, pupylation is carried out by different enzymes that are evolutionarily linked to bacterial carboxylate-amine ligases. Here, we compare the mechanism of Pup-conjugation to target proteins with ubiquitination, describe the evolutionary emergence of pupylation and discuss the importance of this pathway for survival of Mycobacterium tuberculosis in the host. BioMed Central 2012-11-30 /pmc/articles/PMC3511204/ /pubmed/23198822 http://dx.doi.org/10.1186/1741-7007-10-95 Text en Copyright ©2012 Barandun et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Barandun, Jonas Delley, Cyrille L Weber-Ban, Eilika The pupylation pathway and its role in mycobacteria |
title | The pupylation pathway and its role in mycobacteria |
title_full | The pupylation pathway and its role in mycobacteria |
title_fullStr | The pupylation pathway and its role in mycobacteria |
title_full_unstemmed | The pupylation pathway and its role in mycobacteria |
title_short | The pupylation pathway and its role in mycobacteria |
title_sort | pupylation pathway and its role in mycobacteria |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3511204/ https://www.ncbi.nlm.nih.gov/pubmed/23198822 http://dx.doi.org/10.1186/1741-7007-10-95 |
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