Vibrio Iron Transport: Evolutionary Adaptation to Life in Multiple Environments

Autor: Elizabeth E. Wyckoff, Alexandra R. Mey, Shelley M. Payne

Publikováno v: Microbiology and Molecular Biology Reviews. 80:69-90

SUMMARY Iron is an essential element for Vibrio spp., but the acquisition of iron is complicated by its tendency to form insoluble ferric complexes in nature and its association with high-affinity iron-binding proteins in the host. Vibrios occupy a v

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https://doi.org/10.1128/mmbr.00046-15

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

Shigella Iron Transport Systems

Autor: Alexandra R. Mey, Shelley M. Payne, Elizabeth E. Wyckoff

Publikováno v: Shigella: Molecular and Cellular Biology

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::70c780610a62ab29c4e4acd76fe7040d
https://doi.org/10.21775/9781910190197.02

The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand

Autor: Elizabeth E. Wyckoff, Shelley M. Payne

Publikováno v: Molecular Microbiology. 81:1446-1458

Vibrio cholerae, the causative agent of cholera, has an absolute requirement for iron. It transports the catechol siderophores vibriobactin, which it synthesizes and secretes, and enterobactin. These siderophores are transported across the inner memb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d879992c849e3338af57b97731178bfc
https://doi.org/10.1111/j.1365-2958.2011.07775.x

Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex

Autor: Elizabeth E. Wyckoff, Begoña Stevenson, Shelley M. Payne

Publikováno v: Journal of bacteriology. 198(7)

Feo is the major ferrous iron transport system in prokaryotes. Despite having been discovered over 25 years ago and found to be widely distributed among bacteria, Feo is poorly understood, as its structure and mechanism of iron transport have not bee

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fa7c7afa5cd1a90493b81fb62b07899
https://pubmed.ncbi.nlm.nih.gov/26833408