Evidence map›Paper›PMID 2038305›Full record

ArticleMolecular & general genetics : MGG1991

Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein.

Q Chen, E Vierling

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Molecular & general genetics : MGG, 1991. 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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Metabolic Reprogramming in Chloroplasts under Heat Stress in Plants.International journal of molecular sciences · 2018
    Review
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  8. Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.Protein science : a publication of the Protein Society · 2011
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  17. Chloroplast small heat shock proteins: evidence for atypical evolution of an organelle-localized protein.Proceedings of the National Academy of Sciences of the United States of America · 1999
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Q ChenDepartment of Biochemistry, University of Arizona, Tucson 85721.
E Vierling

Funding

Structure/Function of Small Heat Shock ProteinsR01GM042762 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI VIERLING, ELIZABETH · 1989 to 2014
$3.6M
DRS NIH HHS BRSG 507PO-7002NIGMS NIH HHS R01 GM42762-01
6 · The paper itself

Abstract

A low molecular weight heat shock protein which localizes to chloroplasts has been identified in several plant species. This protein belongs to a eukaryotic superfamily of small HSPs, all of which contain a conserved carboxyl-terminal domain. To investigate further the structure of this HSP, we isolated and sequenced cDNA clones for the chloroplast LMW HSPs from Petunia hybrida and Arabidopsis thaliana. The cloning of chloroplast HSPs from these two species enabled us to compare the amino acid sequences of this protein from plant species (petunia, Arabidopsis, pea, soybean and maize) that represent evolutionarily divergent taxonomic subclasses. Three conserved regions were identified, which are designated as regions I, II and III. Regions I and II are also shared by cytoplasmic LMW HSPs and therefore are likely to have functional roles common to all eukaryotic LMW HSPs. In contrast, consensus region III is not found in other LMW HSPs. Secondary structure analysis predicts that this region forms an amphipathic alpha-helix with high conservation of methionine residues on the hydrophobic face and 100% conservation of residues on the hydrophilic face. This structure is similar to three helices, termed "methionine bristles", which are found in a methionine-rich domain of a 54 kDa protein component of signal recognition particle (SRP54). The conservation of regions I and II among LMW cytoplasmic and chloroplast HSPs suggests that these HSPs perform related functions in different cellular compartments. However, identification of the methionine bristle domain suggests that chloroplast HSPs also have unique functions or substrates within the special environment of the chloroplast or other plastids.

Indexed as

Amino Acid SequenceBase SequenceChloroplastsCloning, MolecularDNAHeat-Shock ProteinsMolecular Sequence DataPlantsProtein BiosynthesisProtein ConformationSpecies SpecificityTranscription, GeneticDNAHeat-Shock Proteins

Identifiers

PMID2038305

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.