Evidence map›Paper›PMID 16648249›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Subcellular localization and functions of the barley stem rust resistance receptor-like serine/threonine-specific protein kinase Rpg1.

Jayaveeramuthu Nirmala, Robert Brueggeman, Christina Maier, Christine Clay, Nils Rostoks, C Gamini Kannangara, Diter von Wettstein, Brian J Steffenson, Andris Kleinhofs

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
7.9field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  3. Review
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  8. Article
  9. Tandem Protein Kinases Emerge as New Regulators of Plant Immunity.Molecular plant-microbe interactions : MPMI · 2021
    Review
  10. Genetic transformation of3 Biotech · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Fine mapping and identification of a candidate gene for the barley Un8 true loose smut resistance gene.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2015
    Article
  17. Article
  18. The stem rust resistance gene Rpg5 encodes a protein with nucleotide-binding-site, leucine-rich, and protein kinase domains.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. Article
  20. Article
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

9 authors at 2 institutions in 2 countries.

Jayaveeramuthu NirmalaDepartment of Crop and Soil Sciences, Washingston State University, Pullman, WA 99164, USA.
Robert Brueggeman
Christina Maier
Christine Clay
Nils Rostoks
C Gamini Kannangara
Diter von Wettstein
Brian J Steffenson
Andris Kleinhofs
Crop Research Institute · CZUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rpg1 gene confers resistance to many pathotypes of the stem rust fungus Puccinia graminis f. sp. tritici and has protected barley from serious disease losses for over 60 years. Rpg1 encodes a constitutively expressed protein with two tandem kinase domains. Fractionation by differential centrifugation and aqueous two-phase separation of the microsome proteins located Rpg1 mainly in the cytosol but also in the plasma membrane and intracellular membranes. Recombinant Rpg1 autophosphorylates in vitro intramolecularly only serine and threonine amino acids with a preference for Mn(2+) cations and a K(m) of 0.15 and a V(max) of 0.47 nmol.min(-1).mg(-1) protein. The inability of wild-type Rpg1 to transphosphorylate a recombinant Rpg1 inactivated by site-directed mutation confirmed that Rpg1 autophosphorylation proceeds exclusively via an intramolecular mechanism. Site-directed mutagenesis of the two adjacent lysine residues in the ATP anchor of the two-kinase domains established that the first of the two tandem kinase domains is nonfunctional and that lysine 461 of the second domain is the catalytically active residue. Transgenic barley, expressing Rpg1 mutated in either the kinase 1 or 2 domains, were fully susceptible to P. graminis f. sp. tritici revealing requirement of both kinase domains for resistance. In planta-expressed Rpg1 mutant protein confirmed that mutation in domain 2, but not 1, rendered the protein incapable of autophosphorylation.

Indexed as

Plant DiseasesAmino Acid SequenceCalciumCatalysisCations, DivalentCell MembraneCytoplasmHordeumMagnesiumManganeseMolecular Sequence DataMutagenesis, Site-DirectedPhosphoserinePhosphothreoninePlant ProteinsPlants, Genetically ModifiedCalciumCations, DivalentMagnesiumManganesePhosphoserinePhosphothreoninePlant ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID16648249
PMCPMC1464370
OpenAlexW2033942186

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.