Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A Medicago truncatula Cystathionine-β-Synthase-like Domain-Containing Protein Is Required for Rhizobial Infection and Symbiotic Nitrogen Fixation.

Plant physiology - 1 Apr 2016

Sinharoy Senjuti, Liu Chengwu, Breakspear Andrew, Guan Dian, Shailes Sarah, Nakashima Jin, Zhang Shulan, Wen Jiangqi, Torres-Jerez Ivone, Oldroyd Giles, Murray Jeremy D, Udvardi Michael K

Abstract excerpt

The symbiosis between leguminous plants and soil rhizobia culminates in the formation of nitrogen-fixing organs called nodules that support plant growth. Two Medicago truncatula Tnt1-insertion mutants were identified that produced small nodules, which were unable to fix nitrogen effectively due to ineffective rhizobial colonization. The gene underlying this phenotype was found to encode a protein containing a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cystathionine beta-Synthase
Share to Endocytosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Medicago truncatula

Share to Nitrogen Fixation

Share to Plant Root Nodulation

Share to Rhizobium

Share to Root Nodules, Plant

Share to Symbiosis

Source

Open in PubMed Open full text

Identifiers

PMID: 26884486
DOI: 10.1104/pp.15.01853
PMCID: PMC4825145

Genes

NIN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Medicago truncatula Cystathionine-β-Synthase-like Domain-Containing Protein Is Required for Rhizobial Infection and Symbiotic Nitrogen Fixation.PMID 26884486Read ↗

Rapid identification of causative insertions underlying Medicago truncatula Tnt1 mutants defective in symbiotic nitrogen fixation from a forward genetic screen by whole genome sequencing.Semantic proximity Read ↗

NODULES WITH ACTIVATED DEFENSE 1 is required for maintenance of rhizobial endosymbiosis in Medicago truncatula.Semantic proximity Read ↗

A Medicago truncatula tobacco retrotransposon insertion mutant collection with defects in nodule development and symbiotic nitrogen fixation.Semantic proximity Read ↗

ESN3, a nodule-specific small peptide essential for symbiotic nitrogen fixation in Medicago truncatula.Semantic proximity Read ↗

A nodule-specific protein secretory pathway required for nitrogen-fixing symbiosis.Semantic proximity Read ↗

Rhizobial infection is associated with the development of peripheral vasculature in nodules of Medicago truncatula.Semantic proximity Read ↗

MtSWEET11, a Nodule-Specific Sucrose Transporter of Medicago truncatula.Semantic proximity Read ↗

Antisense repression of the Medicago truncatula nodule-enhanced sucrose synthase leads to a handicapped nitrogen fixation mirrored by specific alterations in the symbiotic transcriptome and metabolome.Semantic proximity Read ↗

MtbHLH1, a bHLH transcription factor involved in Medicago truncatula nodule vascular patterning and nodule to plant metabolic exchanges.Semantic proximity Read ↗

Medicago truncatula esn1 defines a genetic locus involved in nodule senescence and symbiotic nitrogen fixation.Semantic proximity Read ↗

Plant and bacterial symbiotic mutants define three transcriptionally distinct stages in the development of the Medicago truncatula/Sinorhizobium meliloti symbiosis.Semantic proximity Read ↗

Medicago truncatula copper transporter 1 (MtCOPT1) delivers copper for symbiotic nitrogen fixation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.