Evidence map›Paper›PMID 12011353›Full record

ArticlePlant physiology2002

Expression, activation, and biochemical properties of a novel Arabidopsis protein kinase.

Deming Gong, Zhizhong Gong, Yan Guo, Jian-Kang Zhu

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Cold Tolerance ofCurrent issues in molecular biology · 2022
    Article
  3. Plant Calcium Signaling in Response to Potassium Deficiency.International journal of molecular sciences · 2018
    Review
  4. CIPK9 is involved in seed oil regulation inBiotechnology for biofuels · 2018
    Article
  5. Article
  6. Overexpression ofPlant molecular biology reporter · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
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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

4 authors at 1 institution in 1 country.

Deming GongDepartment of Plant Sciences, University of Arizona, Tucson, Arizona 85721, USA.
Zhizhong Gong
Yan Guo
Jian-Kang Zhu
University of Arizona · US

Funding

CALCIUM SIGNALING--INTRACELL ION HOMEOSTASIS REGULATIONR01GM059138 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI ZHU, JIAN-KANG · 1999 to 2015
$4.4M
NIGMS NIH HHS R01 GM059138NIGMS NIH HHS R01GM59138
6 · The paper itself

Abstract

An Arabidopsis SOS2 (salt overly sensitive 2)-like protein kinase gene, PKS6, was expressed in leaves, stems, and siliques, but not detectable in roots of adult plants; its expression in young seedlings was up-regulated by abscisic acid. To determine the biochemical properties of the PKS6 protein, we expressed the PKS6 coding sequence as a glutathione S-transferase fusion protein in Escherichia coli. The bacterially expressed glutathione S-transferase-PKS6 fusion protein was inactive in substrate phosphorylation. We have constructed constitutively active forms of PKS6 by either a deletion of its putative auto-inhibitory FISL motif (i.e. PKS6deltaF) or a substitution of threonine-178 with aspartic acid within the putative activation loop. We found that PKS6deltaF exhibited a strong preference for Mn2+ over Mg2+ as a divalent cation cofactor for kinase activity. PKS6DeltaF displayed substrate specificity against three different peptide substrates and had an optimal pH of approximately 7.5 and temperature optimum of 30 degrees C. The apparent Km values for ATP and the preferred peptide substrate p3 of PKS6deltaF were determined to be 1.7 and 28.5 microM, respectively. These results provide significant insights into the regulation and biochemical properties of the protein kinase PKS6. In addition, the constitutively active, gain-of-function kinase mutants will be invaluable for future determination of the in planta function of PKS6.

Indexed as

Abscisic AcidAmino Acid SequenceArabidopsisArabidopsis ProteinsEscherichia coliFruitGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGlutathione TransferaseHydrogen-Ion ConcentrationMolecular Sequence DataMutationPhosphorylationPlant LeavesPlant StemsProtein KinasesAbscisic AcidArabidopsis ProteinsGlutathione TransferasePKS6 protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSOS2 protein, Arabidopsis

Identifiers

PMID12011353
PMCPMC155886
OpenAlexW2111628857

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.