Evidence map›Paper›PMID 37098975›Full record

ArticleMicrobiology spectrum2023

Coordinated and Distinct Roles of Peptidoglycan Carboxypeptidases DacC and DacA in Cell Growth and Shape Maintenance under Stress Conditions.

Umji Choi, Si Hyoung Park, Han Byeol Lee, Ji Eun Son, Chang-Ro Lee

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.7field-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

15 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
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  11. AlgU mediates hyperosmotic tolerance inApplied and environmental microbiology · 2024
    Article
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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

5 authors at 1 institution in 1 country.

Umji ChoiDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Si Hyoung ParkDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Han Byeol LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Ji Eun SonDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Chang-Ro LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.ORCID 0000-0002-9088-4262
Myongji University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidoglycan (PG) is an essential bacterial architecture pivotal for shape maintenance and adaptation to osmotic stress. Although PG synthesis and modification are tightly regulated under harsh environmental stresses, few related mechanisms have been investigated. In this study, we aimed to investigate the coordinated and distinct roles of the PG dd-carboxypeptidases (DD-CPases) DacC and DacA in cell growth under alkaline and salt stresses and shape maintenance in Escherichia coli. We found that DacC is an alkaline DD-CPase, the enzyme activity and protein stability of which are significantly enhanced under alkaline stress. Both DacC and DacA were required for bacterial growth under alkaline stress, whereas only DacA was required for growth under salt stress. Under normal growth conditions, only DacA was necessary for cell shape maintenance, while under alkaline stress conditions, both DacA and DacC were necessary for cell shape maintenance, but their roles were distinct. Notably, all of these roles of DacC and DacA were independent of ld-transpeptidases, which are necessary for the formation of PG 3-3 cross-links and covalent bonds between PG and the outer membrane lipoprotein Lpp. Instead, DacC and DacA interacted with penicillin-binding proteins (PBPs)-dd-transpeptidases-mostly in a C-terminal domain-dependent manner, and these interactions were necessary for most of their roles. Collectively, our results demonstrate the coordinated and distinct novel roles of DD-CPases in bacterial growth and shape maintenance under stress conditions and provide novel insights into the cellular functions of DD-CPases associated with PBPs.

Indexed as

PeptidoglycanPeptidyl TransferasesBacterial ProteinsCarboxypeptidasesEscherichia coliPenicillin-Binding ProteinsBacterial ProteinsCarboxypeptidasesPenicillin-Binding ProteinsPeptidoglycanPeptidyl Transferasesalkaline stresscell morphologycell shapeDacCdd-carboxypeptidaseld-transpeptidasepenicillin-binding proteinspeptidoglycanpeptidoglycan hydrolasestress adaptation

Identifiers

PMID37098975
PMCPMC10269652
OpenAlexW4367047851

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.