Refactoring the Cryptic Streptophenazine Biosynthetic Gene Cluster Unites Phenazine, Polyketide, and Nonribosomal Peptide Biochemistry

Autor: Victor Nizet, Simone M. Mantovani, Samira Dahesh, Hanna Luhavaya, Bradley S. Moore, Jie Li, Kazuya Murata, Katherine D. Bauman

Publikováno v: Cell Chem Biol

The disconnect between the genomic prediction of secondary metabolite biosynthetic potential and the observed laboratory production profile of microorganisms is well-documented. While heterologous expression of biosynthetic gene clusters (BGCs) is of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0539e7b908afe8f1835b4911319da7c0
https://pubmed.ncbi.nlm.nih.gov/30853419

Minimum Information about a Biosynthetic Gene cluster

Autor: Patrick Caffrey, Renzo Kottmann, Eriko Takano, Sean Doyle, Axel A. Brakhage, Matthew Cummings, Juan Pablo Gomez-Escribano, Yvonne Mast, Ryan F. Seipke, Rob Lavigne, Markus Nett, Hans-Wilhelm Nützmann, Jan Claesen, David H. Sherman, Daniel Petras, Pablo Cruz-Morales, Carl J. Balibar, Anne Osbourn, Oscar P. Kuipers, Leonilde M. Moreira, Xinyu Liu, Marcia S. Osburne, Bohdan Ostash, David P. Fewer, Changsheng Zhang, Pelin Yilmaz, Mohamed S. Donia, Anja Greule, Hyun Uk Kim, Nicholas J. Tobias, Frank Oliver Glöckner, Christoph Geiger, Chia Y. Lee, William H. Gerwick, Philipp Wiemann, Bertolt Gust, Susan E. Jensen, Wilfred A. van der Donk, Jan Kormanec, Ben Shen, Christopher M. Thomas, Jason Micklefield, Srikanth Duddela, R. Cameron Coates, René De Mot, Anthony S. Haines, Neha Garg, Guohui Pan, Roderich D. Süssmuth, Hyung Jin Kwon, Jonathan D. Walton, Lena Gerwick, Jörn Piel, Monika Ehling-Schulz, Zhenhua Tian, Jonathan L. Klassen, Xiaohui Yan, Emily A. Monroe, Yunchang Xie, Russell J. Cox, Keishi Ishida, Grace Yim, Stefano Donadio, Nadine Ziemert, Yuta Tsunematsu, Matthew L. Hillwig, Miroslav Petricek, Sylvie Lautru, Tilmann Weber, Andrew W. Truman, Rainer Breitling, Peter Kötter, Nikos C. Kyrpides, Stephanie Düsterhus, Christian Hertweck, Hideaki Oikawa, Sean F. Brady, Christopher T. Walsh, Adam C. Jones, Marcus A. Moore, Bradley S. Moore, Barrie Wilkinson, Simone M. Mantovani, Nathan A. Moss, Elizabeth E. Wyckoff, Emily P. Balskus, Kapil Tahlan, Fengan Yu, Monica Höfte, Jos M. Raaijmakers, Taifo Mahmud, Yit-Heng Chooi, Yi Tang, Andreas Bechthold, Douglas A. Mitchell, Joanne M. Willey, Helge B. Bode, John B. Biggins, Margherita Sosio, Yi-Qiang Cheng, Carmen Méndez, Leonard Kaysser, Joleen Masschelein, Daniel Krug, Federico Rosconi, Marnix H. Medema, Kaarina Sivonen, Tomohisa Kuzuyama, Mikko Metsä-Ketelä, Esther K. Schmitt, Carsten Kegler, Andriy Luzhetskyy, Gilles P. van Wezel, Bai Linquan, Kai Blin, Jens Nielsen, Bertrand Aigle, Amrita Pati, Harald Gross, Muriel Viaud, Pieter C. Dorrestein, Carla S. Jones, Michael A. Fischbach, Shelley M. Payne, Zhe Rui, Gerard D. Wright, Wen Liu, Alexey V. Melnik, Barry Scott, Brett A. Neilan, Nancy P. Keller, Rainer Borriss, Katrin Jungmann, Michalis Hadjithomas, Evi Stegmann, Daniel J. Edwards, F. Jerry Reen, Alexander Kristian Apel, Wolfgang Wohlleben, Michael J. Smanski, Leonard Katz, Fergal O'Gara, Eric J. N. Helfrich, Sergey B. Zotchev, Olivier Ploux, Arnold J. M. Driessen, Rolf Müller, Jean-Luc Pernodet, K. D. Entian, José A. Salas, Irene de Bruijn, Francisco Barona-Gómez, Jianhua Ju, Jon Clardy

Publikováno v: Nature Chemical Biology, 11(9), 625-631. Nature Publishing Group
Nature Chemical Biology 11 (2015), Nr. 9
Medema, M H, Kottmann, R, Yilmaz, P, Cummings, M, Biggins, J B, Blin, K, Bruijn, I D, Chooi, Y H, Claesen, J, Coates, R C, Cruz-Morales, P, Duddela, S, Düsterhus, S, Edwards, D J, Fewer, D P, Garg, N, Geiger, C, Gomez-Escribano, J P, Greule, A, Hadjithomas, M, Haines, A S, Helfrich, E J N, Hillwig, M L, Ishida, K, Jones, A C, Jones, C S, Jungmann, K, Kegler, C, Kim, H U, Kötter, P, Krug, D, Masschelein, J, Melnik, A V, Mantovani, S M, Monroe, E A, Moore, M, Moss, N, Nützmann, H-W, Pan, G, Pati, A, Petras, D, Reen, F J, Rosconi, F, Rui, Z, Tian, Z, Tobias, N J, Tsunematsu, Y, Wiemann, P, Wyckoff, E, Yan, X, Yim, G, Yu, F, Xie, Y, Aigle, B, Apel, A K, Balibar, C J, Balskus, E P, Barona-Gómez, F, Bechthold, A, Bode, H B, Borriss, R, Brady, S F, Brakhage, A A, Caffrey, P, Cheng, Y-Q, Clardy, J, Cox, R J, Mot, R D, Donadio, S, Donia, M S, Donk, W A V D, Dorrestein, P C, Doyle, S, Driessen, A J M, Ehling-Schulz, M, Entian, K-D, Fischbach, M A, Gerwick, L, Gerwick, W H, Gross, H, Gust, B, Hertweck, C, Höfte, M, Jensen, S E, Ju, J, Katz, L, Kaysser, L, Klassen, J L, Keller, N P, Kormanec, J, Kuipers, O P, Kuzuyama, T, Kyrpides, N C, Kwon, H-J, Lautru, S, Lavigne, R, Lee, C Y, Linquan, B, Liu, X, Liu, W, Luzhetskyy, A, Mahmud, T, Mast, Y, Méndez, C, Metsä-Ketelä, M, Micklefield, J, Mitchell, D A, Moore, B S, Moreira, L M, Müller, R, Neilan, B A, Nett, M, Nielsen, J, O'Gara, F, Oikawa, H, Osbourn, A, Osburne, M S, Ostash, B, Payne, S M, Pernodet, J-L, Petricek, M, Piel, J, Ploux, O, Raaijmakers, J M, Salas, J A, Schmitt, E K, Scott, B, Seipke, R F, Shen, B, Sherman, D H, Sivonen, K, Smanski, M J, Sosio, M, Stegmann, E, Süssmuth, R D, Tahlan, K, Thomas, C M, Tang, Y, Truman, A W, Viaud, M, Walton, J D, Walsh, C T, Weber, T, Wezel, G P V, Wilkinson, B, Willey, J M, Wohlleben, W, Wright, G D, Ziemert, N, Zhang, C, Zotchev, S B, Breitling, R, Takano, E & Glöckner, F O 2015, ' Minimum Information about a Biosynthetic Gene cluster ', Nature chemical biology, vol. 11, pp. 625-631 . https://doi.org/10.1038/nchembio.1890
Medema, M H, Kottmann, R, Yilmaz, P, Cummings, M, Biggins, J B, Blin, K, de Bruijn, I, Kim, H U, Nielsen, J & Weber, T 2015, ' Minimum Information about a Biosynthetic Gene cluster ', Nature Chemical Biology, vol. 11, no. 9, pp. 625-631 . https://doi.org/10.1038/nchembio.1890
ResearcherID
Nature Chemical Biology
Nature Chemical Biology, 2015, 11 (9), pp.625-31. ⟨10.1038/nchembio.1890⟩
Nature Chemical Biology, Nature Publishing Group, 2015, 11 (9), pp.625-31. ⟨10.1038/nchembio.1890⟩
Nature Chemical Biology, 11(9), 625-631
Nature Chemical Biology 11 (2015) 9
Scopus
Medema, M H, Kottmann, R, Yilmaz, P, Cummings, M, Biggins, J B, Blin, K, Bruijn, I D, Chooi, Y H, Claesen, J, Coates, R C, Cruz-Morales, P, Duddela, S, Düsterhus, S, Edwards, D J, Fewer, D P, Garg, N, Geiger, C, Gomez-Escribano, J P, Greule, A, Hadjithomas, M, Haines, A S, Helfrich, E J N, Hillwig, M L, Ishida, K, Jones, A C, Jones, C S, Jungmann, K, Kegler, C, Kim, H U, Kötter, P, Krug, D, Masschelein, J, Melnik, A V, Mantovani, S M, Monroe, E A, Moore, M, Moss, N, Nützmann, H-W, Pan, G, Pati, A, Petras, D, Reen, F J, Rosconi, F, Rui, Z, Tian, Z, Tobias, N J, Tsunematsu, Y, Wiemann, P, Wyckoff, E, Yan, X, Yim, G, Yu, F, Xie, Y, Aigle, B, Apel, A K, Balibar, C J, Balskus, E P, Barona-Gómez, F, Bechthold, A, Bode, H B, Borriss, R, Brady, S F, Brakhage, A A, Caffrey, P, Cheng, Y-Q, Clardy, J, Cox, R J, Mot, R D, Donadio, S, Donia, M S, Donk, W A V D, Dorrestein, P C, Doyle, S, Driessen, A J M, Ehling-Schulz, M, Entian, K-D, Fischbach, M A, Gerwick, L, Gerwick, W H, Gross, H, Gust, B, Hertweck, C, Höfte, M, Jensen, S E, Ju, J, Katz, L, Kaysser, L, Klassen, J L, Keller, N P, Kormanec, J, Kuipers, O P, Kuzuyama, T, Kyrpides, N C, Kwon, H-J, Lautru, S, Lavigne, R, Lee, C Y, Linquan, B, Liu, X, Liu, W, Luzhetskyy, A, Mahmud, T, Mast, Y, Méndez, C, Metsä-Ketelä, M, Micklefield, J, Mitchell, D A, Moore, B S, Moreira, L M, Müller, R, Neilan, B A, Nett, M, Nielsen, J, O'Gara, F, Oikawa, H, Osbourn, A, Osburne, M S, Ostash, B, Payne, S M, Pernodet, J-L, Petricek, M, Piel, J, Ploux, O, Raaijmakers, J M, Salas, J A, Schmitt, E K, Scott, B, Seipke, R F, Shen, B, Sherman, D H, Sivonen, K, Smanski, M J, Sosio, M, Stegmann, E, Süssmuth, R D, Tahlan, K, Thomas, C M, Tang, Y, Truman, A W, Viaud, M, Walton, J D, Walsh, C T, Weber, T, Wezel, G P V, Wilkinson, B, Willey, J M, Wohlleben, W, Wright, G D, Ziemert, N, Zhang, C, Zotchev, S B, Breitling, R, Takano, E & Glöckner, F O 2015, ' Minimum Information about a Biosynthetic Gene cluster ' Nature chemical biology, vol. 11, pp. 625-631 . https://doi.org/10.1038/nchembio.1890
Nature Chemical Biology, Nature Publishing Group, 2015, 11 (9), pp.625-31. 〈10.1038/nchembio.1890〉
RUO. Repositorio Institucional de la Universidad de Oviedo
instname

M.H.M. was supported by a Rubicon fellowship of the Netherlands Organization for Scientific Research (NWO;Rubicon 825.13.001). The work of R.K. was supported by the European Union’s Seventh Framework Programme(Joint Call OCEAN.2011–2: Marine micr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0d1aa4fd11e7fd63b1669a0f6239bbd
https://doi.org/10.1038/nchembio.1890

Flavin-linked oxidase catalyzes pyrrolizine formation of dichloropyrrole-containing polyketide extender unit in chlorizidine A

Autor: Bradley S. Moore, Simone M. Mantovani

Publikováno v: Journal of the American Chemical Society. 135(48)

The marine alkaloid chlorizidine A contains chlorinated pyrroloisoindolone and pyrrolizine rings that are rare chemical features in bacterial natural products. Herein, we report the biosynthetic logic of their construction in Streptomyces sp. CNH-287

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d5a66211bd641bc997864af76d5eaa6
https://pubmed.ncbi.nlm.nih.gov/24246014