Evidence map›Paper›PMID 25128531›Full record

ArticleThe Journal of biological chemistry2014

The crystal structure of the plant small GTPase OsRac1 reveals its mode of binding to NADPH oxidase.

Ken-ichi Kosami, Izuru Ohki, Minoru Nagano, Kyoko Furuita, Toshihiko Sugiki, Yoji Kawano, Tsutomu Kawasaki, Toshimichi Fujiwara, Atsushi Nakagawa, Ko Shimamoto and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

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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

17 citing papers in PubMed, 44 citations in OpenAlex.

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  11. Every Coin Has Two Sides: Reactive Oxygen Species during Rice⁻International journal of molecular sciences · 2019
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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

11 authors at 3 institutions in 1 country.

Ken-ichi KosamiFrom the Institute for Protein Research, Osaka University, Suita, Osaka 565-0871.
Izuru Ohkithe Laboratory of Biophysics and Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, the Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, and ohki.izuru.4a@kyoto-u.ac.jp.
Minoru NaganoLaboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Ikoma, Nara 630-0192.
Kyoko FuruitaFrom the Institute for Protein Research, Osaka University, Suita, Osaka 565-0871.
Toshihiko SugikiFrom the Institute for Protein Research, Osaka University, Suita, Osaka 565-0871.
Yoji KawanoLaboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Ikoma, Nara 630-0192.
Tsutomu KawasakiLaboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, the Department of Advanced Bioscience, Kinki University, Nara 631-8505, Japan.
Toshimichi FujiwaraFrom the Institute for Protein Research, Osaka University, Suita, Osaka 565-0871.
Atsushi NakagawaFrom the Institute for Protein Research, Osaka University, Suita, Osaka 565-0871.
Ko ShimamotoLaboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Ikoma, Nara 630-0192.
Chojiro KojimaFrom the Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, the Laboratory of Biophysics and kojima@protein.osaka-u.ac.jp.
Osaka University · JPNara Institute of Science and Technology · JPKindai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rac/Rop proteins are Rho-type small GTPases that act as molecular switches in plants. Recent studies have identified these proteins as key components in many major plant signaling pathways, such as innate immunity, pollen tube growth, and root hair formation. In rice, the Rac/Rop protein OsRac1 plays an important role in regulating the production of reactive oxygen species (ROS) by the NADPH oxidase OsRbohB during innate immunity. However, the molecular mechanism by which OsRac1 regulates OsRbohB remains unknown. Here, we report the crystal structure of OsRac1 complexed with the non-hydrolyzable GTP analog guanosine 5'-(β,γ-imido)triphosphate at 1.9 Å resolution; this represents the first active-form structure of a plant small GTPase. To elucidate the ROS production in rice cells, structural information was used to design OsRac1 mutants that displayed reduced binding to OsRbohB. Only mutations in the OsRac1 Switch I region showed attenuated interactions with OsRbohB in vitro. In particular, Tyr(39) and Asp(45) substitutions suppressed ROS production in rice cells, indicating that these residues are critical for interaction with and activation of OsRbohB. Structural comparison of active-form OsRac1 with AtRop9 in its GDP-bound inactive form showed a large conformational difference in the vicinity of these residues. Our results provide new insights into the molecular mechanism of the immune response through OsRac1 and the various cellular responses associated with plant Rac/Rop proteins.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCrystallography, X-RayEscherichia coliGene Expression Regulation, PlantGuanylyl ImidodiphosphateModels, MolecularMolecular Sequence DataMonomeric GTP-Binding ProteinsMutationNADPH OxidasesOryzaOxidation-ReductionPhosphatidylinositol PhosphatesArabidopsis ProteinsGuanylyl ImidodiphosphateMonomeric GTP-Binding ProteinsNADPH Oxidasesphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesPlant Proteinsrac1 GTP-Binding ProteinReactive Oxygen SpeciesRecombinant ProteinsROP9 protein, ArabidopsisCrystal StructureNADPH OxidasePlant DefenseRac (Rac GTPase)Rice ImmunitySmall GTPase

Identifiers

PMID25128531
PMCPMC4192507
OpenAlexW2070791372

What OpenQuestion holds

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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.