Evidence map›Paper›PMID 22394314›Full record

ArticleMolecular microbiology2012

The orphan histidine protein kinase SgmT is a c-di-GMP receptor and regulates composition of the extracellular matrix together with the orphan DNA binding response regulator DigR in Myxococcus xanthus.

Tobias Petters, Xin Zhang, Jutta Nesper, Anke Treuner-Lange, Nuria Gomez-Santos, Michael Hoppert, Urs Jenal, Lotte Søgaard-Andersen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.1field-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

29 citing papers in PubMed, 54 citations in OpenAlex.

  1. Milestones in the development ofJournal of bacteriology · 2025
    Review
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  3. Journal of bacteriology · 2023
    Article
  4. Article
  5. Article
  6. Differential ligand-selective control of opposing enzymatic activities within a bifunctional c-di-GMP enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  14. Review
  15. Article
  16. Cyclic di-GMP: second messenger extraordinaire.Nature reviews. Microbiology · 2017
    Review
  17. Article
  18. Article
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  20. 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

8 authors at 2 institutions in 2 countries.

Tobias PettersMax Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043 Marburg, Germany.
Xin Zhang
Jutta Nesper
Anke Treuner-Lange
Nuria Gomez-Santos
Michael Hoppert
Urs Jenal
Lotte Søgaard-Andersen
Max Planck Institute for Terrestrial Microbiology · DEUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Myxococcus xanthus the extracellular matrix is essential for type IV pili-dependent motility and starvation-induced fruiting body formation. Proteins of two-component systems including the orphan DNA binding response regulator DigR are essential in regulating the composition of the extracellular matrix. We identify the orphan hybrid histidine kinase SgmT as the partner kinase of DigR. In addition to kinase and receiver domains, SgmT consists of an N-terminal GAF domain and a C-terminal GGDEF domain. The GAF domain is the primary sensor domain. The GGDEF domain binds the second messenger bis-(3'-5')-cyclic-dimeric-GMP (c-di-GMP) and functions as a c-di-GMP receptor to spatially sequester SgmT. We identify the DigR binding site in the promoter of the fibA gene, which encodes an abundant extracellular matrix metalloprotease. Whole-genome expression profiling experiments in combination with the identified DigR binding site allowed the identification of the DigR regulon and suggests that SgmT/DigR regulates the expression of genes for secreted proteins and enzymes involved in secondary metabolite synthesis. We suggest that SgmT/DigR regulates extracellular matrix composition and that SgmT activity is regulated by two sensor domains with ligand binding to the GAF domain resulting in SgmT activation and c-di-GMP binding to the GGDEF domain resulting in spatial sequestration of SgmT.

Indexed as

Bacterial ProteinsCarrier ProteinsCyclic GMPDNA-Binding ProteinsExtracellular MatrixGene Expression Regulation, BacterialHistidine KinaseIntracellular Signaling Peptides and ProteinsMyxococcus xanthusOligonucleotide Array Sequence AnalysisProtein KinasesRegulonBacterial Proteinsbis(3',5')-cyclic diguanylic acidCarrier ProteinsCyclic GMPcyclic GMP-binding proteinDNA-Binding ProteinsHistidine KinaseIntracellular Signaling Peptides and ProteinsProtein Kinases

Identifiers

PMID22394314
PMCPMC3509222
OpenAlexW2128565626

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.