Evidence map›Paper›PMID 11160079›Full record

ArticleJournal of bacteriology2001

A eukaryotic-type protein kinase, SpkA, is required for normal motility of the unicellular Cyanobacterium synechocystis sp. strain PCC 6803.

A Kamei, T Yuasa, K Orikawa, X X Geng, M Ikeuchi

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 81 citations in OpenAlex.

  1. Type IV pilin regulation: a transcriptional overview.Critical reviews in microbiology · 2026
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  6. Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Revisiting cyanobacterial state transitions.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020
    Review
  9. Article
  10. Review
  11. The CytochromeThe Plant cell · 2019
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Appendages of the cyanobacterial cell.Life (Basel, Switzerland) · 2015
    Review
  20. Microevolution in cyanobacteria: re-sequencing a motile substrain of Synechocystis sp. PCC 6803.DNA research : an international journal for rapid publication of reports on genes and genomes · 2012
    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

5 authors at 1 institution in 1 country.

A KameiDepartment of Life Sciences (Biology), The University of Tokyo, Meguro, Tokyo 153-8902, Japan.
T Yuasa
K Orikawa
X X Geng
M Ikeuchi
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803 comprises many open reading frames (ORFs) which putatively encode eukaryotic-type protein kinase and protein phosphatase. Based on gene disruption analysis, a region of the hypothetical ORF sll1575, which retained a part of the protein kinase motif, was found to be required for normal motility in the original isolate of strain PCC 6803. Sequence determination revealed that in this strain sll1575 was part of a gene (designated spkA) which harbored an entire eukaryotic-type Ser/Thr protein kinase motif. Strain ATCC 27184 and a glucose-tolerant strain derived from the same isolate as the PCC strain had a frameshift mutation dividing spkA into ORFs sll1574 and sll1575. The structural integrity of spkA agreed well with the motility phenotype, determined by colony morphology on agar plates. The spkA gene was expressed in Escherichia coli as a His-tagged protein, which was purified by Ni2+ affinity chromatography. With [gamma-32P]ATP, SpkA was autophosphorylated and transferred the phosphate group to casein, myelin basic protein, and histone. SpkA also phosphorylated several proteins in the membrane fraction of Synechocystis cells. These results suggest that SpkA is a eukaryotic-type Ser/Thr protein kinase and regulates cellular motility via phosphorylation of the membrane proteins in Synechocystis.

Indexed as

Amino Acid SequenceBacterial ProteinsBase SequenceCyanobacteriaEukaryotic CellsMolecular Sequence DataMovementPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSequence Analysis, DNABacterial ProteinsProtein KinasesProtein Serine-Threonine KinasesspkA protein, Synechocystis

Identifiers

PMID11160079
PMCPMC95033
OpenAlexW2119601206

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.