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Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1
Bacterial 3-oxoacyl-ACP reductase (OAR) catalyzes the 3-oxoacyl-ACP reduction step in the fatty acid synthesis pathway. At least 12 genes in the Pseudomonas aeruginosa genome are annotated as OAR-encoding genes. In this study, we characterized the functions of these genes with biochemical and geneti...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6558427/ https://www.ncbi.nlm.nih.gov/pubmed/31231314 http://dx.doi.org/10.3389/fmicb.2019.01028 |
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author | Guo, Qiao-Qiao Zhang, Wen-Bin Zhang, Chao Song, Yu-Lu Liao, Yu-Ling Ma, Jin-Cheng Yu, Yong-Hong Wang, Hai-Hong |
author_facet | Guo, Qiao-Qiao Zhang, Wen-Bin Zhang, Chao Song, Yu-Lu Liao, Yu-Ling Ma, Jin-Cheng Yu, Yong-Hong Wang, Hai-Hong |
author_sort | Guo, Qiao-Qiao |
collection | PubMed |
description | Bacterial 3-oxoacyl-ACP reductase (OAR) catalyzes the 3-oxoacyl-ACP reduction step in the fatty acid synthesis pathway. At least 12 genes in the Pseudomonas aeruginosa genome are annotated as OAR-encoding genes. In this study, we characterized the functions of these genes with biochemical and genetic techniques. With the exception of PA2967, which encodes FabG, an essential protein in fatty acid synthesis, only the PA4389 and PA4786 gene products had OAR activity, and the single deletion of these two genes reduced the ability of P. aeruginosa to produce several specific quorum-sensing (QS) signals. However, PA4389 and PA4786 do not have key roles in fatty acid synthesis. Moreover, although most OAR homologs had no OAR activity, some may function in carbon utilization. The PA3128 product may play a role in the TCA cycle, and PA0182 and PA1470 seem to be required for the utilization of several amino acids. The rest of the OAR homologs have no roles in carbon utilization, but the deletion of one of these genes might affect the production of virulence factors by P. aeruginosa. We conclude that most OAR homolog genes do not encode OAR enzymes, and that these proteins do not function in fatty acid synthesis. IMPORTANCE: We report that although all P. aeruginosa OAR homologs have similar structures and the conserved catalytic triad of the bacterial OAR enzymes, only a few OAR homologs have OAR activity. |
format | Online Article Text |
id | pubmed-6558427 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-65584272019-06-21 Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 Guo, Qiao-Qiao Zhang, Wen-Bin Zhang, Chao Song, Yu-Lu Liao, Yu-Ling Ma, Jin-Cheng Yu, Yong-Hong Wang, Hai-Hong Front Microbiol Microbiology Bacterial 3-oxoacyl-ACP reductase (OAR) catalyzes the 3-oxoacyl-ACP reduction step in the fatty acid synthesis pathway. At least 12 genes in the Pseudomonas aeruginosa genome are annotated as OAR-encoding genes. In this study, we characterized the functions of these genes with biochemical and genetic techniques. With the exception of PA2967, which encodes FabG, an essential protein in fatty acid synthesis, only the PA4389 and PA4786 gene products had OAR activity, and the single deletion of these two genes reduced the ability of P. aeruginosa to produce several specific quorum-sensing (QS) signals. However, PA4389 and PA4786 do not have key roles in fatty acid synthesis. Moreover, although most OAR homologs had no OAR activity, some may function in carbon utilization. The PA3128 product may play a role in the TCA cycle, and PA0182 and PA1470 seem to be required for the utilization of several amino acids. The rest of the OAR homologs have no roles in carbon utilization, but the deletion of one of these genes might affect the production of virulence factors by P. aeruginosa. We conclude that most OAR homolog genes do not encode OAR enzymes, and that these proteins do not function in fatty acid synthesis. IMPORTANCE: We report that although all P. aeruginosa OAR homologs have similar structures and the conserved catalytic triad of the bacterial OAR enzymes, only a few OAR homologs have OAR activity. Frontiers Media S.A. 2019-05-22 /pmc/articles/PMC6558427/ /pubmed/31231314 http://dx.doi.org/10.3389/fmicb.2019.01028 Text en Copyright © 2019 Guo, Zhang, Zhang, Song, Liao, Ma, Yu and Wang. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Guo, Qiao-Qiao Zhang, Wen-Bin Zhang, Chao Song, Yu-Lu Liao, Yu-Ling Ma, Jin-Cheng Yu, Yong-Hong Wang, Hai-Hong Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 |
title | Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 |
title_full | Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 |
title_fullStr | Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 |
title_full_unstemmed | Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 |
title_short | Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes in Pseudomonas aeruginosa PAO1 |
title_sort | characterization of 3-oxacyl-acyl carrier protein reductase homolog genes in pseudomonas aeruginosa pao1 |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6558427/ https://www.ncbi.nlm.nih.gov/pubmed/31231314 http://dx.doi.org/10.3389/fmicb.2019.01028 |
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