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Quantitative proteomics of a B12 -dependent alga grown in coculture with bacteria reveals metabolic tradeoffs required for mutualism.
Helliwell, Katherine E; Pandhal, Jagroop; Cooper, Matthew B et al.
2018In New Phytologist, 217 (2), p. 599 - 612
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Mots-clés :
Lobomonas rostrata; Mesorhizobium loti; iTRAQ proteomics; mutualism; photosynthesis; vitamin B12; Algal Proteins; Amino Acids; RNA, Messenger; Vitamin B 12; Algal Proteins/metabolism; Amino Acids/metabolism; Chlorophyta/drug effects; Chlorophyta/genetics; Chlorophyta/growth & development; Chlorophyta/metabolism; Coculture Techniques; Computational Biology; Electron Transport/drug effects; Gene Expression Regulation, Plant/drug effects; Mesorhizobium/drug effects; Mesorhizobium/growth & development; Photosynthesis/drug effects; RNA, Messenger/genetics; RNA, Messenger/metabolism; Symbiosis/drug effects; Vitamin B 12/pharmacology; Proteomics; Chlorophyta; Electron Transport; Gene Expression Regulation, Plant; Mesorhizobium; Symbiosis; Physiology; Plant Science; vitamin B-12
Résumé :
[en] The unicellular green alga Lobomonas rostrata requires an external supply of vitamin B12 (cobalamin) for growth, which it can obtain in stable laboratory cultures from the soil bacterium Mesorhizobium loti in exchange for photosynthate. We investigated changes in protein expression in the alga that allow it to engage in this mutualism. We used quantitative isobaric tagging (iTRAQ) proteomics to determine the L. rostrata proteome grown axenically with B12 supplementation or in coculture with M. loti. Data are available via ProteomeXchange (PXD005046). Using the related Chlamydomonas reinhardtii as a reference genome, 588 algal proteins could be identified. Enzymes of amino acid biosynthesis were higher in coculture than in axenic culture, and this was reflected in increased amounts of total cellular protein and several free amino acids. A number of heat shock proteins were also elevated. Conversely, photosynthetic proteins and those of chloroplast protein synthesis were significantly lower in L. rostrata cells in coculture. These observations were confirmed by measurement of electron transfer rates in cells grown under the two conditions. The results indicate that, despite the stability of the mutualism, L. rostrata experiences stress in coculture with M. loti, and must adjust its metabolism accordingly.
Disciplines :
Sciences aquatiques & océanologie
Auteur, co-auteur :
Helliwell, Katherine E;  Department of Plant Sciences, University of Cambridge, Cambridge, CB2 3EA, UK
Pandhal, Jagroop;  Department of Chemical and Biological Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK
Cooper, Matthew B;  Department of Plant Sciences, University of Cambridge, Cambridge, CB2 3EA, UK
LONGWORTH, Joseph  ;  Department of Chemical and Biological Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK
Kudahl, Ulrich Johan;  Department of Plant Sciences, University of Cambridge, Cambridge, CB2 3EA, UK
Russo, David A ;  Department of Chemical and Biological Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK
Tomsett, Eleanor V;  Department of Plant Sciences, University of Cambridge, Cambridge, CB2 3EA, UK
Bunbury, Freddy;  Department of Plant Sciences, University of Cambridge, Cambridge, CB2 3EA, UK
Salmon, Deborah L;  Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, EX4 4QD, UK
Smirnoff, Nicholas;  Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, EX4 4QD, UK
Wright, Phillip C;  Department of Chemical and Biological Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK
Smith, Alison G;  Department of Plant Sciences, University of Cambridge, Cambridge, CB2 3EA, UK
Co-auteurs externes :
yes
Langue du document :
Anglais
Titre :
Quantitative proteomics of a B12 -dependent alga grown in coculture with bacteria reveals metabolic tradeoffs required for mutualism.
Date de publication/diffusion :
janvier 2018
Titre du périodique :
New Phytologist
ISSN :
0028-646X
eISSN :
1469-8137
Maison d'édition :
Blackwell Publishing Ltd, England
Volume/Tome :
217
Fascicule/Saison :
2
Pagination :
599 - 612
Peer reviewed :
Peer reviewed vérifié par ORBi
Organisme subsidiant :
Engineering and Physical Sciences Research Council
Biotechnology and Biological Sciences Research Council
Natural Environment Research Council
Engineering and Physical Sciences Research Council
EU Framework Programme
Biotechnology and Biological Sciences Research Council
Natural Environment Research Council
Subventionnement (détails) :
The work in this manuscript was supported by funding from the Biotechnology and Biological Sciences Research Council (BBSRC) of the UK (grant BB/I013164/1, a CASE studentship for M.B.C. joint with PML Applications Ltd, Plymouth, UK, and a DTP studentship for F.B.); an EU FP7 Marie Curie ITN Photo.Comm, no. 317184 for U.J.K.; Engineering and Physical Science Research Council (EPSRC) grant EP/E036252/1; and the Natural Environment Research Council (NERC) grant NE/J024767/1.
Disponible sur ORBilu :
depuis le 19 décembre 2023

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