Cited by 97Bacterial biofilms and quorum sensingBacterial Genetics and BiotechnologyEscherichia coli research studies

SiaA and SiaD are essential for inducing autoaggregation as a specific response to detergent stress in Pseudomonas aeruginosa

Open access
Klebensberger, Janosch, Birkenmaier, Antoinette, Geffers, Robert, Kjelleberg, Staffan, Philipp, Bodo·2009·Environmental Microbiology

Abstract

Cell aggregation is a stress response and serves as a survival strategy for Pseudomonas aeruginosa strain PAO1 during growth with the toxic detergent Na-dodecylsulfate (SDS). This process involves the psl operon and is linked to c-di-GMP signalling. The induction of cell aggregation in response to SDS was studied. Transposon and site-directed mutagenesis revealed that the cupA-operon and the co-transcribed genes siaA (PA0172) and siaD (PA0169) were essential for SDS-induced aggregation. While siaA encodes a putative membrane protein with a HAMP and a PP2C-like phosphatase domain, siaD encodes a putative diguanylate cyclase involved in the biosynthesis of c-di-GMP. Complementation studies uncovered that the loss of SDS-induced aggregation in the formerly isolated spontaneous mutant strain N was caused by a non-functional siaA allele. DNA-microarray analysis of SDS-grown cells revealed consistent activation of eight genes, including cupA1, with known or presumptive important functions in cell aggregation in the parent strain compared with non-aggregating siaA and siaD mutants. A siaAD-dependent increase of cupA1 mRNA levels in SDS-grown cells was also shown by Northern blots. These results clearly demonstrate that SiaAD are essential for inducing cell aggregation as a specific response to SDS and suggest that they are responsible for perceiving and transducing SDS-related stress.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1111/j.1462-2920.2009.02012.x

Cites

60 of 60 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • SiaD is predicted to encode a putative cytoplasmic di-guanylate cyclase involved in the biosynthesis of cyclic di-guanosine monophosphate (c-di-GMP).

    “SiaD is predicted to encode a putative cytoplasmic di-guanylate cyclase involved in the biosynthesis of cyclic di-guanosine monophosphate (c-di-GMP), thus suggesting that SDS-induced aggregation is regulated through a c-di-GMP-dependent signal transduction pathway [108].”

    From Bacterial autoaggregation (2018) · cites this paper as [108]

  • SDS-induced aggregation in P. aeruginosa is regulated through a c-di-GMP-dependent signal transduction pathway.

    “SiaD is predicted to encode a putative cytoplasmic di-guanylate cyclase involved in the biosynthesis of cyclic di-guanosine monophosphate (c-di-GMP), thus suggesting that SDS-induced aggregation is regulated through a c-di-GMP-dependent signal transduction pathway [108].”

    From Bacterial autoaggregation (2018) · cites this paper as [108]

  • The genes siaA and siaD are essential for induction of autoaggregation as a specific response to SDS in P. aeruginosa.

    “The genes siaA (SDS-induced-aggregation A) and siaD are essential for induction of autoaggregation as a specific response to SDS and have been suggested to be responsible for perceiving and transducing SDS-related stress [108].”

    From Bacterial autoaggregation (2018) · cites this paper as [108]

  • SiaA encodes a putative membrane protein harboring a HAMP domain and a PP2C-like phosphatase domain.

    “SiaA encodes a putative membrane protein harboring a HAMP (histidine kinases, adenylyl cyclases, methyl-accepting chemotaxis proteins and phosphatases) domain and a PP2C (Protein phosphatase 2C)-like phosphatase domain.”

    From Bacterial autoaggregation (2018) · cites this paper as [108]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

  • Bacterial autoaggregation

    Trunk, T., Bacterial Cell Surface Group, S. F. G. A. E. B., S. Khalil, H., & C. Leo, J. (2018) · AIMS Microbiology · doi:10.3934/microbiol.2018.1.140 · Cited by 444 · see citing works

    “of autoaggregation as a specific response to SDS and have been suggested to be responsible for perceiving and transducing SDS-related stress [108].”
    Background

Authors
Klebensberger, J., Birkenmaier, A., Geffers, R., Kjelleberg, S., & Philipp, B.
Affiliations
  • University of Konstanz (DE)
  • Helmholtz Centre for Infection Research (DE)
  • UNSW Sydney (AU)
Corresponding author
Philipp, Bodo
Venue
Environmental Microbiology
Publisher
Wiley
Published
2009-12
Volume
11
Issue
12
Pages
3073-3086
ISSN
  • 1462-2912 (ISSN-L)
  • 1462-2920
OpenAlex
W2132171052
Cited by
97
References
60
Citations by year
2026: 3 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 6 · 2021: 9 · 2020: 13 · 2019: 6 · 2018: 6 · 2017: 4 · 2016: 10 · 2015: 7 · 2014: 7 · 2013: 7 · 2012: 3
FWCI
1.07
Type
journal article
Language
en
Open access
Locations
  • Environmental Microbiology (publishedVersion)
  • PubMed (publishedVersion)
  • KOPS (University of Konstanz) (submittedVersion)
  • HZI (Helmholtz Centre for Infection Research) (submittedVersion)
Funders
  • Deutsche Forschungsgemeinschaft (SFB 454)
  • Universität Konstanz
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
Keywords
Pseudomonas aeruginosa, cell aggregation, self-aggregation, sodium dodecyl sulfate, c-di-GMP signalling, diguanylate cyclase, HAMP domain, stress response, gene expression
MeSH terms
Detergents, Genes, Bacterial, Mutation, Pseudomonas aeruginosa, Sodium Dodecyl Sulfate, Stress, Physiological, Gene Expression Regulation, Bacterial

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review