Evidence map›Paper›PMID 19127371›Full record

ArticleMolecular genetics and genomics : MGG2009

Conserved inserts in the Hsp60 (GroEL) and Hsp70 (DnaK) proteins are essential for cellular growth.

Bhag Singh, Radhey S Gupta

Abstract read
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In one paragraph

Article in Molecular genetics and genomics : MGG, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

40 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
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  5. Phylogenomic and molecular marker based studies to clarify the evolutionary relationships amongstInternational journal of systematic and evolutionary microbiology · 2024
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  8. Temperature Matters: Bacterial Response to Temperature Change.Journal of microbiology (Seoul, Korea) · 2023
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  9. Article
  10. Cytoplasmic molecular chaperones in Pseudomonas species.Journal of microbiology (Seoul, Korea) · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. LeveragingFrontiers in microbiology · 2021
    Review
  17. Review
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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

2 authors at 1 institution in 1 country.

Bhag SinghDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, L8N 3Z5, Canada.
Radhey S Gupta
McMaster University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hsp60 and Hsp70 chaperones contain a number of conserved inserts that are restricted to particular phyla of bacteria. A one aa insert in the E. coli GroEL and a 21-23 insert in the DnaK proteins are specific for most Gram-negative bacteria. Two other inserts in DnaK are limited to certain groups of proteobacteria. The requirement of these inserts for cellular growth was examined by carrying out complementation studies with temperature-sensitive (T(s)) mutants of E. coli groEL or dnaK. Our results demonstrate that deletion or most changes in these inserts completely abolished the complementation ability of the mutant proteins. Studies with GroEL and DnaK from some other species that either lacked or contained these inserts also indicated that these inserts are essential for growth of E. coli. The DnaK from some bacteria contains a two aa insert that is not found in E. coli. Introduction of this insert into the E. coli DnaK also led to its inactivation, indicating that these inserts are specific for different groups. We postulate that these conserved inserts that are localized in loop regions on protein surfaces, are involved in some ancillary functions that are essential for the groups of bacteria where they are found.

Indexed as

Amino Acid SequenceBacteriaChaperonin 60Conserved SequenceEscherichia coliEscherichia coli ProteinsEvolution, MolecularGenes, BacterialGenetic Complementation TestHSP70 Heat-Shock ProteinsModels, MolecularMolecular Sequence DataMutagenesis, InsertionalMutationProtein Structure, TertiaryRecombinant ProteinsChaperonin 60dnaK protein, E coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsRecombinant Proteins

Identifiers

PMID19127371
OpenAlexW1987175113

What OpenQuestion holds

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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.