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Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane
While many data are available on genes encoding proteins for degradation of hydrocarbons in bacteria, the impact of alkane on transporter protein expression is unclear. Pseudomonas aeruginosa SJTD-1 is a strain that can consume medium- and long-chain n-alkanes. In order to study the proteins involve...
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/PMC5491041/ https://www.ncbi.nlm.nih.gov/pubmed/28662172 http://dx.doi.org/10.1371/journal.pone.0179842 |
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author | Zhou, Xuefeng Xing, Xuejiao Hou, Jingli Liu, Jianhua |
author_facet | Zhou, Xuefeng Xing, Xuejiao Hou, Jingli Liu, Jianhua |
author_sort | Zhou, Xuefeng |
collection | PubMed |
description | While many data are available on genes encoding proteins for degradation of hydrocarbons in bacteria, the impact of alkane on transporter protein expression is unclear. Pseudomonas aeruginosa SJTD-1 is a strain that can consume medium- and long-chain n-alkanes. In order to study the proteins involved in n-octadecane uptake, we use iTRAQ and label free comparative proteomics analysis to identify the proteins of alkane uptake in response to n-octadecane (C18) comparing with n-hexadecane (C16) in P. aeruginosa SJTD-1. A total of 1102 and 1249 proteins were identified by iTRAQ-based and label free quantitative methodologies, respectively. By application of 1.5 (iTRAQ) or 2-fold (label free) for upregulated and 0.65 (iTRAQ) or 0.5-fold (label free) for downregulated cutoff values, 91 and 99 proteins were found to be differentially expressed comparing SJTD-1 cultivated on C18 with C16 respectively. There are six proteins with the common differential expression by iTRAQ and label free-based methods. Results of bioinformational analysis suggested the involvement of bacterial chemotaxis in responds to C18. Additionally, quantitative reverse transcriptase PCR (qRT-PCR) results confirmed C18-induced change in levels of FleQ, FliC, NirS, FadL and FadD proteins and the role of the proteins in n-octadecane uptake was further discussed in P. aeruginosa. In conclusion, results of the present study provided information about possible target-related proteins of bacterial chemotaxis, swimming performance, alkane transport to stimulus of n-ctadecane rather than n-hexadecane in P. aeruginosa SJTD-1. |
format | Online Article Text |
id | pubmed-5491041 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-54910412017-07-18 Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane Zhou, Xuefeng Xing, Xuejiao Hou, Jingli Liu, Jianhua PLoS One Research Article While many data are available on genes encoding proteins for degradation of hydrocarbons in bacteria, the impact of alkane on transporter protein expression is unclear. Pseudomonas aeruginosa SJTD-1 is a strain that can consume medium- and long-chain n-alkanes. In order to study the proteins involved in n-octadecane uptake, we use iTRAQ and label free comparative proteomics analysis to identify the proteins of alkane uptake in response to n-octadecane (C18) comparing with n-hexadecane (C16) in P. aeruginosa SJTD-1. A total of 1102 and 1249 proteins were identified by iTRAQ-based and label free quantitative methodologies, respectively. By application of 1.5 (iTRAQ) or 2-fold (label free) for upregulated and 0.65 (iTRAQ) or 0.5-fold (label free) for downregulated cutoff values, 91 and 99 proteins were found to be differentially expressed comparing SJTD-1 cultivated on C18 with C16 respectively. There are six proteins with the common differential expression by iTRAQ and label free-based methods. Results of bioinformational analysis suggested the involvement of bacterial chemotaxis in responds to C18. Additionally, quantitative reverse transcriptase PCR (qRT-PCR) results confirmed C18-induced change in levels of FleQ, FliC, NirS, FadL and FadD proteins and the role of the proteins in n-octadecane uptake was further discussed in P. aeruginosa. In conclusion, results of the present study provided information about possible target-related proteins of bacterial chemotaxis, swimming performance, alkane transport to stimulus of n-ctadecane rather than n-hexadecane in P. aeruginosa SJTD-1. Public Library of Science 2017-06-29 /pmc/articles/PMC5491041/ /pubmed/28662172 http://dx.doi.org/10.1371/journal.pone.0179842 Text en © 2017 Zhou 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 Zhou, Xuefeng Xing, Xuejiao Hou, Jingli Liu, Jianhua Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane |
title | Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane |
title_full | Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane |
title_fullStr | Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane |
title_full_unstemmed | Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane |
title_short | Quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of Pseudomonas aeruginosa SJTD-1 in response to n-octadecane and n-hexadecane |
title_sort | quantitative proteomics analysis of proteins involved in alkane uptake comparing the profiling of pseudomonas aeruginosa sjtd-1 in response to n-octadecane and n-hexadecane |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5491041/ https://www.ncbi.nlm.nih.gov/pubmed/28662172 http://dx.doi.org/10.1371/journal.pone.0179842 |
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