Evidence map›Paper›PMID 9811909›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

A PII-like protein in Arabidopsis: putative role in nitrogen sensing.

M H Hsieh, H M Lam, F J van de Loo, G Coruzzi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
16.9field-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

83 citing papers in PubMed, 237 citations in OpenAlex.

  1. Review
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  10. International journal of molecular sciences · 2021
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  13. Effect ofJournal of agricultural and food chemistry · 2020
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  14. Frontiers in microbiology · 2020
    Article
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23 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 3 countries.

M H HsiehDepartment of Biology, New York University, New York, NY 10003, USA.
H M Lam
F J van de Loo
G Coruzzi
Commonwealth Scientific and Industrial Research Organisation · AUNew York University · USPlant Industry · AU

Funding

REGULATION OF AMINO ACID BIOSYNTHESIS GENES IN PLANTSR01GM032877 · NIGMS · ROCKEFELLER UNIVERSITY · PI CORUZZI, GLORIA · 1985 to 2012
$4.8M
NIGMS NIH HHS GM32877NIGMS NIH HHS R01 GM032877
6 · The paper itself

Abstract

PII is a protein allosteric effector in Escherichia coli and other bacteria that indirectly regulates glutamine synthetase at the transcriptional and post-translational levels in response to nitrogen availability. Data supporting the notion that plants have a nitrogen regulatory system(s) includes previous studies showing that the levels of mRNA for plant nitrogen assimilatory genes such as glutamine synthetase (GLN) and asparagine synthetase (ASN) are modulated by carbon and organic nitrogen metabolites. Here, we have characterized a PII homolog (GLB1) in two higher plants, Arabidopsis thaliana and Ricinus communis (Castor bean). Each plant PII-like protein has high overall identity to E. coli PII (50%). Western blot analyses reveal that the plant PII-like protein is a nuclear-encoded chloroplast protein. The PII-like protein of plants appears to be regulated at the transcriptional level in that levels of GLB1 mRNA are affected by light and metabolites. To initiate studies of the in vivo function of the Arabidopsis PII-like protein, we have constructed transgenic lines in which PII expression is uncoupled from its native regulation. Analyses of these transgenic plants support the notion that the plant PII-like protein may serve as part of a complex signal transduction network involved in perceiving the status of carbon and organic nitrogen. Thus, the PII protein found in archaea, bacteria, and now in higher eukaryotes (plants) is one of the most widespread regulatory proteins known, providing evidence for an ancestral metabolic regulatory mechanism that may have existed before the divergence of these three domains of life.

Indexed as

Amino Acid SequenceArabidopsisBacterial ProteinsGenes, PlantMolecular Sequence DataNitrogenPII Nitrogen Regulatory ProteinsPlant ProteinsPlants, Genetically ModifiedSequence AlignmentSequence AnalysisBacterial ProteinsNitrogenPIID regulatory protein, BacteriaPII Nitrogen Regulatory ProteinsPlant Proteins

Identifiers

PMID9811909
PMCPMC24990
OpenAlexW2042380638

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.