Relationship between the Rod complex and peptidoglycan structure in Escherichia coli
Abstract Peptidoglycan for elongation in Escherichia coli is synthesized by the Rod complex, which includes RodZ. Although various mutant strains of the Rod complex have been isolated, the relationship between the activity of the Rod complex and the overall physical and chemical structures of the pe...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2023-10-01
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| Series: | MicrobiologyOpen |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/mbo3.1385 |
| _version_ | 1797649943557570560 |
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| author | Risa Ago Yuhei O. Tahara Honoka Yamaguchi Motoya Saito Wakana Ito Kaito Yamasaki Taishi Kasai Sho Okamoto Taiki Chikada Taku Oshima Issey Osaka Makoto Miyata Hironori Niki Daisuke Shiomi |
| author_facet | Risa Ago Yuhei O. Tahara Honoka Yamaguchi Motoya Saito Wakana Ito Kaito Yamasaki Taishi Kasai Sho Okamoto Taiki Chikada Taku Oshima Issey Osaka Makoto Miyata Hironori Niki Daisuke Shiomi |
| author_sort | Risa Ago |
| collection | DOAJ |
| description | Abstract Peptidoglycan for elongation in Escherichia coli is synthesized by the Rod complex, which includes RodZ. Although various mutant strains of the Rod complex have been isolated, the relationship between the activity of the Rod complex and the overall physical and chemical structures of the peptidoglycan have not been reported. We constructed a RodZ mutant, termed RMR, and analyzed the growth rate, morphology, and other characteristics of cells producing the Rod complexes containing RMR. The growth and morphology of RMR cells were abnormal, and we isolated suppressor mutants from RMR cells. Most of the suppressor mutations were found in components of the Rod complex, suggesting that these suppressor mutations increase the integrity and/or the activity of the Rod complex. We purified peptidoglycan from wild‐type, RMR, and suppressor mutant cells and observed their structures in detail. We found that the peptidoglycan purified from RMR cells had many large holes and different compositions of muropeptides from those of WT cells. The Rod complex may be a determinant not only for the whole shape of peptidoglycan but also for its highly dense structure to support the mechanical strength of the cell wall. |
| first_indexed | 2024-03-11T15:54:23Z |
| format | Article |
| id | doaj.art-d41ae6e1f42f427d9c2f50654f83cdcd |
| institution | Directory Open Access Journal |
| issn | 2045-8827 |
| language | English |
| last_indexed | 2024-03-11T15:54:23Z |
| publishDate | 2023-10-01 |
| publisher | Wiley |
| record_format | Article |
| series | MicrobiologyOpen |
| spelling | doaj.art-d41ae6e1f42f427d9c2f50654f83cdcd2023-10-25T12:16:30ZengWileyMicrobiologyOpen2045-88272023-10-01125n/an/a10.1002/mbo3.1385Relationship between the Rod complex and peptidoglycan structure in Escherichia coliRisa Ago0Yuhei O. Tahara1Honoka Yamaguchi2Motoya Saito3Wakana Ito4Kaito Yamasaki5Taishi Kasai6Sho Okamoto7Taiki Chikada8Taku Oshima9Issey Osaka10Makoto Miyata11Hironori Niki12Daisuke Shiomi13Department of Life Science, College of Science Rikkyo University Tokyo JapanGraduate School of Science Osaka Metropolitan University Osaka JapanDepartment of Life Science, College of Science Rikkyo University Tokyo JapanDepartment of Biotechnology, Faculty of Engineering Toyama Prefectural University Imizu Toyama JapanDepartment of Biotechnology, Faculty of Engineering Toyama Prefectural University Imizu Toyama JapanDepartment of Pharmaceutical Engineering, Faculty of Engineering Toyama Prefectural University Imizu Toyama JapanDepartment of Life Science, College of Science Rikkyo University Tokyo JapanMicrobial Physiology Laboratory, Department of Gene Function and Phenomics National Institute of Genetics Mishima Shizuoka JapanDepartment of Life Science, College of Science Rikkyo University Tokyo JapanDepartment of Biotechnology, Faculty of Engineering Toyama Prefectural University Imizu Toyama JapanDepartment of Pharmaceutical Engineering, Faculty of Engineering Toyama Prefectural University Imizu Toyama JapanGraduate School of Science Osaka Metropolitan University Osaka JapanMicrobial Physiology Laboratory, Department of Gene Function and Phenomics National Institute of Genetics Mishima Shizuoka JapanDepartment of Life Science, College of Science Rikkyo University Tokyo JapanAbstract Peptidoglycan for elongation in Escherichia coli is synthesized by the Rod complex, which includes RodZ. Although various mutant strains of the Rod complex have been isolated, the relationship between the activity of the Rod complex and the overall physical and chemical structures of the peptidoglycan have not been reported. We constructed a RodZ mutant, termed RMR, and analyzed the growth rate, morphology, and other characteristics of cells producing the Rod complexes containing RMR. The growth and morphology of RMR cells were abnormal, and we isolated suppressor mutants from RMR cells. Most of the suppressor mutations were found in components of the Rod complex, suggesting that these suppressor mutations increase the integrity and/or the activity of the Rod complex. We purified peptidoglycan from wild‐type, RMR, and suppressor mutant cells and observed their structures in detail. We found that the peptidoglycan purified from RMR cells had many large holes and different compositions of muropeptides from those of WT cells. The Rod complex may be a determinant not only for the whole shape of peptidoglycan but also for its highly dense structure to support the mechanical strength of the cell wall.https://doi.org/10.1002/mbo3.1385cell shapepeptidoglycanRod complexsuppressor mutation |
| spellingShingle | Risa Ago Yuhei O. Tahara Honoka Yamaguchi Motoya Saito Wakana Ito Kaito Yamasaki Taishi Kasai Sho Okamoto Taiki Chikada Taku Oshima Issey Osaka Makoto Miyata Hironori Niki Daisuke Shiomi Relationship between the Rod complex and peptidoglycan structure in Escherichia coli MicrobiologyOpen cell shape peptidoglycan Rod complex suppressor mutation |
| title | Relationship between the Rod complex and peptidoglycan structure in Escherichia coli |
| title_full | Relationship between the Rod complex and peptidoglycan structure in Escherichia coli |
| title_fullStr | Relationship between the Rod complex and peptidoglycan structure in Escherichia coli |
| title_full_unstemmed | Relationship between the Rod complex and peptidoglycan structure in Escherichia coli |
| title_short | Relationship between the Rod complex and peptidoglycan structure in Escherichia coli |
| title_sort | relationship between the rod complex and peptidoglycan structure in escherichia coli |
| topic | cell shape peptidoglycan Rod complex suppressor mutation |
| url | https://doi.org/10.1002/mbo3.1385 |
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