Evidence map›Paper›PMID 8097278›Full record

ArticleMolecular and cellular biology1993

Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins.

E M Hallberg, Y Shu, R L Hallberg

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Review
  6. Article
  7. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.International journal of molecular sciences · 2018
    Article
  8. Electron transport chain in a thermotolerant yeast.Journal of bioenergetics and biomembranes · 2017
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
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  15. Article
  16. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

E M HallbergDepartment of Biology, Syracuse University, New York 13244.
Y Shu
R L Hallberg
Syracuse University · US

Funding

MOLECULAR ANALYSIS OF A MITOCHONDRIAL ASSEMBLY FACTORR01GM046302 · NIGMS · SYRACUSE UNIVERSITY AT SYRACUSE · PI HALLBERG, RICHARD L · 1991 to 1994
–
NIGMS NIH HHS R01 GM46302
6 · The paper itself

Abstract

We have created yeast strains in which the mitochondrial chaperonin, hsp60, can be either physically depleted or functionally inactivated. Cells completely depleted of hsp60 stop growing but retain for awhile the capacity to reaccumulate hsp60. While this newly made hsp60 is targeted to and processed correctly within the mitochondrion, assembly of a functional hsp60 complex does not occur. Rather, the hsp60 monomers are localized in different-size soluble complexes containing another mitochondrial chaperone, the mitochondrial form of hsp70. A number of other mitochondrial matrix-targeted proteins synthesized in the absence of functional hsp60 are imported into mitochondria but often show some buildup of precursor forms and, unlike hsp60, accumulate as insoluble aggregates. By contrast, several mitochondrial proteins normally targeted to the intermembrane space show normal processing in the complete absence of a functional hsp60 complex. Similar and complementary results were obtained when we examined the metabolism of matrix- and intermembrane space-localized proteins in cells expressing three different temperature-sensitive alleles of HSP60. In all cases, matrix-targeted proteins synthesized at nonpermissive (i.e., hsp60-inactivating) temperatures were correctly targeted to and processed within mitochondria but accumulated predominantly or totally as insoluble aggregates. The metabolism of two intermembrane space proteins, cytochrome b2 and cytochrome c1, was unaffected at the nonpermissive temperature, as judged by the correct processing and complete solubility of newly synthesized forms of both proteins. These findings are discussed with regard to current models of intermembrane targeting.

Indexed as

Blotting, WesternChaperonin 60Gene DeletionGenes, FungalHeat-Shock ProteinsKineticsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)MitochondriaMutagenesisSaccharomyces cerevisiaeSpecies SpecificityTemperatureChaperonin 60Heat-Shock ProteinsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)

Identifiers

PMID8097278
PMCPMC359697
OpenAlexW1839052904

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.