Evidence map›Paper›PMID 27534419›Full record

ArticlePlant molecular biology2016

Split-ubiquitin yeast two-hybrid interaction reveals a novel interaction between a natural resistance associated macrophage protein and a membrane bound thioredoxin in Brassica juncea.

Ananya Marik, Haraprasad Naiya, Madhumanti Das, Gairik Mukherjee, Soumalee Basu, Chinmay Saha, Rajdeep Chowdhury, Kankan Bhattacharyya, Anindita Seal

Abstract read
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Article in Plant molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Ananya MarikDepartment of Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India.
Haraprasad NaiyaDepartment of Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India.
Madhumanti DasDepartment of Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India.
Gairik MukherjeeDepartment of Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India.
Soumalee BasuDepartment of Microbiology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India.
Chinmay SahaDepartment of Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India.
Rajdeep ChowdhuryDepartment of Physical Chemistry, Indian Association for the Cultivation of Science, 2A and 2B Raja S.C Mullick Road, Jadavpur, Kolkata, 700032, India.
Kankan BhattacharyyaDepartment of Physical Chemistry, Indian Association for the Cultivation of Science, 2A and 2B Raja S.C Mullick Road, Jadavpur, Kolkata, 700032, India.
Anindita SealDepartment of Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata, 700019, India. aninditaseal@gmail.com.
University of Calcutta · INIndian Association for the Cultivation of Science · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural resistance associated macrophage proteins (NRAMPs) are evolutionarily conserved metal transporters involved in the transport of essential and nonessential metals in plants. Fifty protein interactors of a Brassica juncea NRAMP protein was identified by a Split-Ubiquitin Yeast-Two-Hybrid screen. The interactors were predicted to function as components of stress response, signaling, development, RNA binding and processing. BjNRAMP4.1 interactors were particularly enriched in proteins taking part in photosynthetic or light regulated processes, or proteins predicted to be localized in plastid/chloroplast. Further, many interactors also had a suggested role in cellular redox regulation. Among these, the interaction of a photosynthesis-related thioredoxin, homologous to Arabidopsis HCF164 (High-chlorophyll fluorescence164) was studied in detail. Homology modeling of BjNRAMP4.1 suggested that it could be redox regulated by BjHCF164. In yeast, the interaction between the two proteins was found to increase in response to metal deficiency; Mn excess and exogenous thiol. Excess Mn also increased the interaction in planta and led to greater accumulation of the complex at the root apoplast. Network analysis of Arabidopsis homologs of BjNRAMP4.1 interactors showed enrichment of many protein components, central to chloroplastic/cellular ROS signaling. BjNRAMP4.1 interacted with BjHCF164 at the root membrane and also in the chloroplast in accordance with its proposed function related to photosynthesis, indicating that this interaction occurred at different sub-cellular locations depending on the tissue. This may serve as a link between metal homeostasis and chloroplastic/cellular ROS through protein-protein interaction.

Indexed as

ArabidopsisGene Expression Regulation, PlantMustard PlantThioredoxinsTwo-Hybrid System TechniquesUbiquitinThioredoxinsUbiquitinMetal stressNRAMPProtein–protein interactionRedoxThioredoxin

Identifiers

PMID27534419
OpenAlexW2507222194

What OpenQuestion holds

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Registered trials

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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.