Evidence map›Paper›PMID 35481628›Full record

ArticleProtein science : a publication of the Protein Society2022

Prevalent association with the bacterial cell envelope of prokaryotic expansins revealed by bioinformatics analysis.

Andrés de Sandozequi, Juan José Salazar-Cortés, Irán Tapia-Vázquez, Claudia Martínez-Anaya

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

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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

6 citing papers in PubMed.

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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

4 authors.

Andrés de SandozequiDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, UNAM, Av. Universidad 2001, Chamilpa, Cuernavaca, Morelos, Mexico.ORCID 0000-0002-7387-9883
Juan José Salazar-CortésDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, UNAM, Av. Universidad 2001, Chamilpa, Cuernavaca, Morelos, Mexico.
Irán Tapia-VázquezDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, UNAM, Av. Universidad 2001, Chamilpa, Cuernavaca, Morelos, Mexico.ORCID 0000-0003-0399-0751
Claudia Martínez-AnayaDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, UNAM, Av. Universidad 2001, Chamilpa, Cuernavaca, Morelos, Mexico.ORCID 0000-0002-2483-6115

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expansins are a group of proteins from diverse organisms from bacteria to plants. Although expansins show structural conservation, their biological roles seem to differ among kingdoms. In plants, these proteins remodel the cell wall during plant growth and other processes. Contrarily, determination of bacterial expansin activity has proven difficult, although genetic evidence of bacterial mutants indicates that expansins participate in bacteria-plant interactions. Nevertheless, a large proportion of expansin genes are found in the genomes of free-living bacteria, suggesting roles that are independent of the interaction with living plants. Here, we analyzed all available sequences of prokaryotic expansins for correlations between surface electric charge, extra protein modules, and sequence motifs for association with the bacteria exterior after export. Additionally, information on the fate of protein after translocation across the membrane also points to bacterial cell association of expansins through six different mechanisms, such as attachment of a lipid molecule for membrane anchoring in diderm species or covalent linking to the peptidoglycan layer in monoderms such as the Bacilliales. Our results have implications for expansin function in the context of bacteria-plant interactions and also for free-living species in which expansins might affect cell-cell or cell-substrate interaction properties and indicate the need to re-examine the roles currently considered for these proteins.

Indexed as

Computational BiologyPlant ProteinsBacteriaCell MembraneCell WallPlantsPlant Proteinsbacterial expansincell envelopeisoelectric pointprotein domainsignal peptide

Identifiers

PMID35481628
PMCPMC9045087

What OpenQuestion holds

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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.