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Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor
The general secretion (Sec) pathway plays a prominent role in bacterial protein export, and the accessory component SecDF has been shown to improve transportation efficiency. Inspection of Streptomyces coelicolor genome reveals the unexpected presence of two different forms of secDF homologous genes...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4139356/ https://www.ncbi.nlm.nih.gov/pubmed/25140821 http://dx.doi.org/10.1371/journal.pone.0105237 |
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author | Zhou, Zhan Li, Yudong Sun, Ning Sun, Zhihao Lv, Longxian Wang, Yufeng Shen, Libing Li, Yong-Quan |
author_facet | Zhou, Zhan Li, Yudong Sun, Ning Sun, Zhihao Lv, Longxian Wang, Yufeng Shen, Libing Li, Yong-Quan |
author_sort | Zhou, Zhan |
collection | PubMed |
description | The general secretion (Sec) pathway plays a prominent role in bacterial protein export, and the accessory component SecDF has been shown to improve transportation efficiency. Inspection of Streptomyces coelicolor genome reveals the unexpected presence of two different forms of secDF homologous genes: one in fused form (secDF) and the other in separated form (secD and secF). However, the functional role of two SecDF homologs in S. coelicolor has not yet been determined. Transcriptional analysis of secDF homologs reveals that these genes are constitutively expressed. However, the transcript levels of secD and secF are much higher than that of secDF in S. coelicolor. Deletion of secDF or/and secD/secF in S. coelicolor did result in reduced secretion efficiency of Xylanase A and Amylase C, suggesting that they may have redundant functions for Sec-dependent translocation pathway. Moreover, our results also indicate that SecD/SecF plays a more prominent role than SecDF in protein translocation. Evolutionary analysis suggests that the fused and separated SecDF homologs in Streptomyces may have disparate evolutionary ancestries. SecD/SecF may be originated from vertical transmission of existing components from ancestor of Streptomyces species. However, SecDF may be derived from bacterial ancestors through horizontal gene transfer. Alternately, it is also plausible that SecDF may have arisen through additional gene duplication and fusion events. The acquisition of a second copy may confer a selective benefit to Streptomyces by enhancing protein transport capacity. Taken together, our results provide new insights into the potential biological function and evolutionary aspects of the prokaryotic SecDF complex. |
format | Online Article Text |
id | pubmed-4139356 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-41393562014-08-25 Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor Zhou, Zhan Li, Yudong Sun, Ning Sun, Zhihao Lv, Longxian Wang, Yufeng Shen, Libing Li, Yong-Quan PLoS One Research Article The general secretion (Sec) pathway plays a prominent role in bacterial protein export, and the accessory component SecDF has been shown to improve transportation efficiency. Inspection of Streptomyces coelicolor genome reveals the unexpected presence of two different forms of secDF homologous genes: one in fused form (secDF) and the other in separated form (secD and secF). However, the functional role of two SecDF homologs in S. coelicolor has not yet been determined. Transcriptional analysis of secDF homologs reveals that these genes are constitutively expressed. However, the transcript levels of secD and secF are much higher than that of secDF in S. coelicolor. Deletion of secDF or/and secD/secF in S. coelicolor did result in reduced secretion efficiency of Xylanase A and Amylase C, suggesting that they may have redundant functions for Sec-dependent translocation pathway. Moreover, our results also indicate that SecD/SecF plays a more prominent role than SecDF in protein translocation. Evolutionary analysis suggests that the fused and separated SecDF homologs in Streptomyces may have disparate evolutionary ancestries. SecD/SecF may be originated from vertical transmission of existing components from ancestor of Streptomyces species. However, SecDF may be derived from bacterial ancestors through horizontal gene transfer. Alternately, it is also plausible that SecDF may have arisen through additional gene duplication and fusion events. The acquisition of a second copy may confer a selective benefit to Streptomyces by enhancing protein transport capacity. Taken together, our results provide new insights into the potential biological function and evolutionary aspects of the prokaryotic SecDF complex. Public Library of Science 2014-08-20 /pmc/articles/PMC4139356/ /pubmed/25140821 http://dx.doi.org/10.1371/journal.pone.0105237 Text en © 2014 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, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Zhou, Zhan Li, Yudong Sun, Ning Sun, Zhihao Lv, Longxian Wang, Yufeng Shen, Libing Li, Yong-Quan Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor |
title | Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor
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title_full | Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor
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title_fullStr | Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor
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title_full_unstemmed | Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor
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title_short | Function and Evolution of Two Forms of SecDF Homologs in Streptomyces coelicolor
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title_sort | function and evolution of two forms of secdf homologs in streptomyces coelicolor |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4139356/ https://www.ncbi.nlm.nih.gov/pubmed/25140821 http://dx.doi.org/10.1371/journal.pone.0105237 |
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