Evidence map›Paper›PMID 14996794›Full record

ArticleJournal of bacteriology2004

Temperature regulation of the hemin storage (Hms+) phenotype of Yersinia pestis is posttranscriptional.

Robert D Perry, Alexander G Bobrov, Olga Kirillina, Heather A Jones, Lisa Pedersen, Jennifer Abney, Jacqueline D Fetherston

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Yersinia pestis ΔApplied and environmental microbiology · 2023
    Article
  3. Review
  4. Deletion of Yersinia pestisJournal of bacteriology · 2021
    Article
  5. Article
  6. Article
  7. Inactivation of theMicroorganisms · 2020
    Article
  8. Article
  9. Frontiers in cellular and infection microbiology · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Antibody to a conserved antigenic target is protective against diverse prokaryotic and eukaryotic pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. Cyclic di-GMP: the first 25 years of a universal bacterial second messenger.Microbiology and molecular biology reviews : MMBR · 2013
    Review
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

7 authors at 1 institution in 1 country.

Robert D PerryDepartment of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, Kentucky 40536, USA. rperry@pop.uky.edu
Alexander G Bobrov
Olga Kirillina
Heather A Jones
Lisa Pedersen
Jennifer Abney
Jacqueline D Fetherston
University of Kentucky · US

Funding

Plague biofilm formation--regulation and functionR01AI025098 · NIAID · UNIVERSITY OF KENTUCKY · PI PERRY, ROBERT DONALD · 1993 to 2013
$2.9M
IRON STORAGE AND UPTAKE IN YERSINIA PESTISR29AI025098 · NIAID · UNIVERSITY OF KENTUCKY · PI PERRY, ROBERT DONALD · 1988 to 1992
–
NIAID NIH HHS AI25098NIAID NIH HHS R01 AI025098
6 · The paper itself

Abstract

In Yersinia pestis, the Congo red (and hemin) binding that is characteristic of the Hms+ phenotype occurs at temperatures up to 34 degrees C but not at higher temperatures. Manifestation of the Hms+ phenotype requires at least five proteins (HmsH, -F, -R, -S, and -T) that are organized into two separate operons: hmsHFRS and hmsT. HmsH and HmsF are outer membrane proteins, while HmsR, HmsS, and HmsT are predicted to be inner membrane proteins. We have used transcriptional reporter constructs, RNA dot blots, and Western blots to examine the expression of hms operons and proteins. Our studies indicate that transcription from the hmsHFRS and hmsT promoters is not regulated by the iron status of the cells, growth temperature, or any of the Hms proteins. In addition, the level of mRNA for both operons is not significantly affected by growth temperature. However, protein levels of HmsH, HmsR, and HmsT in cells grown at 37 degrees C are very low compared to those in cells grown at 26 degrees C, while the amounts of HmsF and HmsS show only a moderate reduction at the higher growth temperature. Neither the Pla protease nor a putative endopeptidase (Y2360) encoded upstream of hmsH is essential for temperature regulation of the Hms+ phenotype. However, HmsT at 37 degrees C is sensitive to degradation by Lon and/or ClpPX. Thus, the stability of HmsH, HmsR, and HmsT proteins likely plays a role in temperature regulation of the Hms+ phenotype of Y. pestis.

Indexed as

Gene Expression Regulation, BacterialTranscription, GeneticBacterial ProteinsCulture MediaHeminMembrane ProteinsMutationOperonPhenotypePlasmidsTemperatureYersinia pestisBacterial ProteinsCulture MediaHeminHmsR protein, Yersinia pestisHMST protein, Yersinia pestisMembrane Proteins

Identifiers

PMID14996794
PMCPMC355957
OpenAlexW2143499105

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.