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Hu, B.* ; Hänsch, R.* ; Grunau, K.* ; Hohtanz, L.* ; Kucklick, M.* ; Grünig, N.* ; Haensch, V.G.* ; Liu, R.* ; Peng, T.* ; Wiebicke, M.* ; Fard, I.S.* ; Messerer, M. ; Gädeke, F.* ; Stradal, T.E.B.* ; Milatz, M.* ; Hertweck, C.* ; Engelmann, S.* ; Rennenberg, H.* ; Oliphant, K.D.*

Symbiotic peptides modulate rhizobial physiology without terminal differentiation.

Sci. Adv. 12:eaed2816 (2026)
Publ. Version/Full Text Research data DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
Symbiotic nitrogen fixation reduces reliance on synthetic fertilizers and is central to agriculture and ecosystem functioning. In legumes, this process occurs in root nodules where rhizobia differentiate into bacteroids that either remain viable or undergo terminal differentiation, a strategy that can enhance nitrogen fixation but limits nodule life span. This irreversible program suits annual legumes and has evolved convergently across multiple lineages, including the inverted repeat-lacking clade (IRLC), where it is enforced by nodule-specific cysteine-rich (NCR) peptides. By contrast, perennial legumes with indeterminate nodules must sustain symbiosis over extended periods, which is incompatible with terminally differentiated bacteroids. Here, we identify a family of nodule-specific proline-glycine-rich peptides (NPGs) in Robinia that are induced upon rhizobial infection. NPGs are highly expressed in nodules, encode intrinsically disordered peptides, and accumulate in infected cells within the fixation zone. Exposure of Mesorhizobium robiniae to recombinant NPGs induces transcriptional changes associated with a fixation-related physiological state while preserving bacterial viability. These findings identify NPGs as candidate host effectors at the plant-microbe interface and point to an alternative mode of symbiont modulation in perennial legumes.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Rhizobia ; Symbiosis ; Nitrogen Fixation ; Root Nodule ; Effector ; Perennial Plant ; Rhizobium
ISSN (print) / ISBN 2375-2548
e-ISSN 2375-2548
Quellenangaben Volume: 12, Issue: 26, Pages: , Article Number: eaed2816 Supplement: ,
Publisher American Association for the Advancement of Science (AAAS)
Publishing Place Washington, DC [u.a.]
Reviewing status Peer reviewed