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dc.contributor.authorSankari, Siva
dc.contributor.authorBabu, Vignesh MP
dc.contributor.authorBian, Ke
dc.contributor.authorAlhhazmi, Areej
dc.contributor.authorAndorfer, Mary C
dc.contributor.authorAvalos, Dante M
dc.contributor.authorSmith, Tyler A
dc.contributor.authorYoon, Kwan
dc.contributor.authorDrennan, Catherine L
dc.contributor.authorYaffe, Michael B
dc.contributor.authorLourido, Sebastian
dc.contributor.authorWalker, Graham C
dc.date.accessioned2023-03-07T16:26:30Z
dc.date.available2023-03-07T16:26:30Z
dc.date.issued2022
dc.identifier.urihttps://hdl.handle.net/1721.1/148391
dc.description.abstractSymbiotic partnerships with rhizobial bacteria enable legumes to grow without nitrogen fertilizer because rhizobia convert atmospheric nitrogen gas into ammonia via nitrogenase. After Sinorhizobium meliloti penetrate the root nodules that they have elicited in Medicago truncatula, the plant produces a family of about 700 nodule cysteine-rich (NCR) peptides that guide the differentiation of endocytosed bacteria into nitrogen-fixing bacteroids. The sequences of the NCR peptides are related to the defensin class of antimicrobial peptides, but have been adapted to play symbiotic roles. Using a variety of spectroscopic, biophysical and biochemical techniques, we show here that the most extensively characterized NCR peptide, 24 amino acid NCR247, binds haem with nanomolar affinity. Bound haem molecules and their iron are initially made biologically inaccessible through the formation of hexamers (6 haem/6 NCR247) and then higher-order complexes. We present evidence that NCR247 is crucial for effective nitrogen-fixing symbiosis. We propose that by sequestering haem and its bound iron, NCR247 creates a physiological state of haem deprivation. This in turn induces an iron-starvation response in rhizobia that results in iron import, which itself is required for nitrogenase activity. Using the same methods as for L-NCR247, we show that the D-enantiomer of NCR247 can bind and sequester haem in an equivalent manner. The special abilities of NCR247 and its D-enantiomer to sequester haem suggest a broad range of potential applications related to human health.en_US
dc.language.isoen
dc.publisherSpringer Science and Business Media LLCen_US
dc.relation.isversionof10.1038/S41564-022-01192-Yen_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alikeen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/en_US
dc.sourcePMCen_US
dc.titleA haem-sequestering plant peptide promotes iron uptake in symbiotic bacteriaen_US
dc.typeArticleen_US
dc.identifier.citationSankari, Siva, Babu, Vignesh MP, Bian, Ke, Alhhazmi, Areej, Andorfer, Mary C et al. 2022. "A haem-sequestering plant peptide promotes iron uptake in symbiotic bacteria." Nature Microbiology, 7 (9).
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biology
dc.contributor.departmentHoward Hughes Medical Institute
dc.contributor.departmentWhitehead Institute for Biomedical Research
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineering
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistry
dc.contributor.departmentCenter for Precision Cancer Medicine
dc.relation.journalNature Microbiologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2023-03-07T15:57:03Z
dspace.orderedauthorsSankari, S; Babu, VMP; Bian, K; Alhhazmi, A; Andorfer, MC; Avalos, DM; Smith, TA; Yoon, K; Drennan, CL; Yaffe, MB; Lourido, S; Walker, GCen_US
dspace.date.submission2023-03-07T15:57:08Z
mit.journal.volume7en_US
mit.journal.issue9en_US
mit.licenseOPEN_ACCESS_POLICY
mit.metadata.statusAuthority Work and Publication Information Neededen_US


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