Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane
Secretins form large multimeric pores in the outer membrane (OM) of Gram-negative bacteria. These pores are part of type II and III secretion systems (T2SS and T3SS, respectively) and are crucial for pathogenicity. Recent structural studies indicate that secretins form a structure rich in β-strands....
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| Format: | Article |
| Language: | English |
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Shared Science Publishers OG
2019-11-01
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| Series: | Microbial Cell |
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| Online Access: | http://microbialcell.com/researcharticles/2019a-natarajan-microbial-cell/ |
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| author | Janani Natarajan Anasuya Moitra Sussanne Zabel Nidhi Singh Samuel Wagner Doron Rapaport |
| author_facet | Janani Natarajan Anasuya Moitra Sussanne Zabel Nidhi Singh Samuel Wagner Doron Rapaport |
| author_sort | Janani Natarajan |
| collection | DOAJ |
| description | Secretins form large multimeric pores in the outer membrane (OM) of Gram-negative bacteria. These pores are part of type II and III secretion systems (T2SS and T3SS, respectively) and are crucial for pathogenicity. Recent structural studies indicate that secretins form a structure rich in β-strands. However, little is known about the mechanism by which secretins assemble into the OM. Based on the conservation of the biogenesis of β-barrel proteins in bacteria and mitochondria, we used yeast cells as a model system to study the assembly process of secretins. To that end, we analyzed the biogenesis of PulD (T2SS), SsaC (T3SS) and InvG (T3SS) in wild type cells or in cells mutated for known mitochondrial import and assembly factors. Our results suggest that secretins can be expressed in yeast cells, where they are enriched in the mitochondrial fraction. Interestingly, deletion of mitochondrial import receptors like Tom20 and Tom70 reduces the mitochondrial association of PulD but does not affect that of InvG. SsaC shows another dependency pattern and its membrane assembly is enhanced by the absence of Tom70 and compromised in cells lacking Tom20 or the topogenesis of outer membrane β-barrel proteins (TOB) complex component, Mas37. Collectively, these findings suggest that various secretins can follow different pathways to assemble into the bacterial OM. |
| format | Article |
| id | doaj-art-3e0cf1cb912445f8bfe261ac5677c9cf |
| institution | DOAJ |
| issn | 2311-2638 |
| language | English |
| publishDate | 2019-11-01 |
| publisher | Shared Science Publishers OG |
| record_format | Article |
| series | Microbial Cell |
| spelling | doaj-art-3e0cf1cb912445f8bfe261ac5677c9cf2025-08-20T02:57:37ZengShared Science Publishers OGMicrobial Cell2311-26382019-11-0171152710.15698/mic2020.01.703Yeast can express and assemble bacterial secretins in the mitochondrial outer membraneJanani Natarajan0Anasuya Moitra1Sussanne Zabel2Nidhi Singh3Samuel Wagner4Doron Rapaport5Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.Interfaculty Institute of Microbiology and Infection Medicine (IMIT), University of Tübingen, Tübingen, Germany.Interfaculty Institute of Microbiology and Infection Medicine (IMIT), University of Tübingen, Tübingen, Germany.Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.Secretins form large multimeric pores in the outer membrane (OM) of Gram-negative bacteria. These pores are part of type II and III secretion systems (T2SS and T3SS, respectively) and are crucial for pathogenicity. Recent structural studies indicate that secretins form a structure rich in β-strands. However, little is known about the mechanism by which secretins assemble into the OM. Based on the conservation of the biogenesis of β-barrel proteins in bacteria and mitochondria, we used yeast cells as a model system to study the assembly process of secretins. To that end, we analyzed the biogenesis of PulD (T2SS), SsaC (T3SS) and InvG (T3SS) in wild type cells or in cells mutated for known mitochondrial import and assembly factors. Our results suggest that secretins can be expressed in yeast cells, where they are enriched in the mitochondrial fraction. Interestingly, deletion of mitochondrial import receptors like Tom20 and Tom70 reduces the mitochondrial association of PulD but does not affect that of InvG. SsaC shows another dependency pattern and its membrane assembly is enhanced by the absence of Tom70 and compromised in cells lacking Tom20 or the topogenesis of outer membrane β-barrel proteins (TOB) complex component, Mas37. Collectively, these findings suggest that various secretins can follow different pathways to assemble into the bacterial OM.http://microbialcell.com/researcharticles/2019a-natarajan-microbial-cell/invgmitochondriaouter membraneprotein sortingpuldsecretinsssac |
| spellingShingle | Janani Natarajan Anasuya Moitra Sussanne Zabel Nidhi Singh Samuel Wagner Doron Rapaport Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane Microbial Cell invg mitochondria outer membrane protein sorting puld secretins ssac |
| title | Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane |
| title_full | Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane |
| title_fullStr | Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane |
| title_full_unstemmed | Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane |
| title_short | Yeast can express and assemble bacterial secretins in the mitochondrial outer membrane |
| title_sort | yeast can express and assemble bacterial secretins in the mitochondrial outer membrane |
| topic | invg mitochondria outer membrane protein sorting puld secretins ssac |
| url | http://microbialcell.com/researcharticles/2019a-natarajan-microbial-cell/ |
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