Evidence map›Paper›PMID 26401024›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Rhizobial peptidase HrrP cleaves host-encoded signaling peptides and mediates symbiotic compatibility.

Paul A Price, Houston R Tanner, Brett A Dillon, Mohammed Shabab, Graham C Walker, Joel S Griffitts

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
19.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 107 citations in OpenAlex.

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  14. Legumes Regulate Symbiosis with Rhizobia via Their Innate Immune System.International journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Paul A PriceDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT 84602;
Houston R TannerDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT 84602;
Brett A DillonDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT 84602;
Mohammed ShababDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
Graham C WalkerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
Joel S GriffittsDepartment of Microbiology and Molecular Biology, Brigham Young University, Provo, UT 84602; joelg@byu.edu.
Brigham Young University · USMassachusetts Institute of Technology · US

Funding

MOLEULAR GENETICS OF RHIZOBIUM PLASMIDSR01GM031030 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WALKER, GRAHAM C · 1985 to 2020
$8.6M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
NIGMS NIH HHS P41 GM103311NIGMS NIH HHS P41-GM103311NIGMS NIH HHS R01 GM031030
6 · The paper itself

Abstract

Legume-rhizobium pairs are often observed that produce symbiotic root nodules but fail to fix nitrogen. Using the Sinorhizobium meliloti and Medicago truncatula symbiotic system, we previously described several naturally occurring accessory plasmids capable of disrupting the late stages of nodule development while enhancing bacterial proliferation within the nodule. We report here that host range restriction peptidase (hrrP), a gene found on one of these plasmids, is capable of conferring both these properties. hrrP encodes an M16A family metallopeptidase whose catalytic activity is required for these symbiotic effects. The ability of hrrP to suppress nitrogen fixation is conditioned upon the genotypes of both the host plant and the hrrP-expressing rhizobial strain, suggesting its involvement in symbiotic communication. Purified HrrP protein is capable of degrading a range of nodule-specific cysteine-rich (NCR) peptides encoded by M. truncatula. NCR peptides are crucial signals used by M. truncatula for inducing and maintaining rhizobial differentiation within nodules, as demonstrated in the accompanying article [Horváth B, et al. (2015) Proc Natl Acad Sci USA, 10.1073/pnas.1500777112]. The expression pattern of hrrP and its effects on rhizobial morphology are consistent with the NCR peptide cleavage model. This work points to a symbiotic dialogue involving a complex ensemble of host-derived signaling peptides and bacterial modifier enzymes capable of adjusting signal strength, sometimes with exploitative outcomes.

Indexed as

Protein Sorting SignalsSymbiosisMolecular Sequence DataNitrogen FixationPeptide HydrolasesProteolysisTranscription, GeneticPeptide HydrolasesProtein Sorting SignalsmetallopeptidaseNCR peptidesnitrogen fixationsymbiosis

Identifiers

PMID26401024
PMCPMC4679054
OpenAlexW1696748403

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.