Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439
Cytochrome P450 enzymes (CYPs or P450s) and ferredoxins (Fdxs) are ubiquitously distributed in all domains of life. Bacterial P450s are capable of catalyzing various oxidative reactions with two electrons usually donated by Fdxs. Particularly in Streptomyces, there are abundant P450s that have exhib...
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Elsevier
2024-12-01
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| Series: | Engineering Microbiology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667370324000286 |
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| author | Shuai Li Zhong Li Guoqiang Zhang Vlada B. Urlacher Li Ma Shengying Li |
| author_facet | Shuai Li Zhong Li Guoqiang Zhang Vlada B. Urlacher Li Ma Shengying Li |
| author_sort | Shuai Li |
| collection | DOAJ |
| description | Cytochrome P450 enzymes (CYPs or P450s) and ferredoxins (Fdxs) are ubiquitously distributed in all domains of life. Bacterial P450s are capable of catalyzing various oxidative reactions with two electrons usually donated by Fdxs. Particularly in Streptomyces, there are abundant P450s that have exhibited outstanding biosynthetic capacity of bioactive metabolites and great potential for xenobiotic metabolisms. However, no systematic study has been conducted on physiological functions of the whole cytochrome P450 complement (CYPome) and ferredoxin complement (Fdxome) of any Streptomyces strain to date, leaving a significant knowledge gap in microbial functional genomics. Herein, we functionally analyze the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 by investigating groups of single and sequential P450 deletion mutants, single P450 overexpression mutants, and Fdx gene deletion or repression mutants. Construction of an unprecedented P450-null mutant strain indicates that none of P450 genes are essential for S. venezuelae in maintaining its survival and normal morphology. The non-housekeeping Fdx1 and housekeeping Fdx3 not only jointly support the cellular activity of the prototypic P450 enzyme PikC, but also play significant regulatory functions. These findings significantly advance the understandings of the native functionality of P450s and Fdxs as well as their cellular interactions. |
| format | Article |
| id | doaj-art-e09da32c648f41f2be003c7ddcbcb874 |
| institution | OA Journals |
| issn | 2667-3703 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Engineering Microbiology |
| spelling | doaj-art-e09da32c648f41f2be003c7ddcbcb8742025-08-20T01:57:04ZengElsevierEngineering Microbiology2667-37032024-12-014410016610.1016/j.engmic.2024.100166Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439Shuai Li0Zhong Li1Guoqiang Zhang2Vlada B. Urlacher3Li Ma4Shengying Li5State Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, ChinaInstitute of Biochemistry, Heinrich-Heine-University Düsseldorf, Universitätsstraße 1, Düsseldorf 40225, GermanyState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China; Corresponding authors.State Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China; Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao, Shandong 266237, China; Corresponding authors.Cytochrome P450 enzymes (CYPs or P450s) and ferredoxins (Fdxs) are ubiquitously distributed in all domains of life. Bacterial P450s are capable of catalyzing various oxidative reactions with two electrons usually donated by Fdxs. Particularly in Streptomyces, there are abundant P450s that have exhibited outstanding biosynthetic capacity of bioactive metabolites and great potential for xenobiotic metabolisms. However, no systematic study has been conducted on physiological functions of the whole cytochrome P450 complement (CYPome) and ferredoxin complement (Fdxome) of any Streptomyces strain to date, leaving a significant knowledge gap in microbial functional genomics. Herein, we functionally analyze the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 by investigating groups of single and sequential P450 deletion mutants, single P450 overexpression mutants, and Fdx gene deletion or repression mutants. Construction of an unprecedented P450-null mutant strain indicates that none of P450 genes are essential for S. venezuelae in maintaining its survival and normal morphology. The non-housekeeping Fdx1 and housekeeping Fdx3 not only jointly support the cellular activity of the prototypic P450 enzyme PikC, but also play significant regulatory functions. These findings significantly advance the understandings of the native functionality of P450s and Fdxs as well as their cellular interactions.http://www.sciencedirect.com/science/article/pii/S2667370324000286StreptomycesCytochrome P450 enzymesCYPomeFerredoxinFdxomePikC |
| spellingShingle | Shuai Li Zhong Li Guoqiang Zhang Vlada B. Urlacher Li Ma Shengying Li Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 Engineering Microbiology Streptomyces Cytochrome P450 enzymes CYPome Ferredoxin Fdxome PikC |
| title | Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 |
| title_full | Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 |
| title_fullStr | Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 |
| title_full_unstemmed | Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 |
| title_short | Functional analysis of the whole CYPome and Fdxome of Streptomyces venezuelae ATCC 15439 |
| title_sort | functional analysis of the whole cypome and fdxome of streptomyces venezuelae atcc 15439 |
| topic | Streptomyces Cytochrome P450 enzymes CYPome Ferredoxin Fdxome PikC |
| url | http://www.sciencedirect.com/science/article/pii/S2667370324000286 |
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