Evidence map›Paper›PMID 38842932›Full record

ArticleNucleic acids research2024

YjgA plays dual roles in enhancing PTC maturation.

Mengtan Du, Chenke Deng, Ting Yu, Qixin Zhou, Fuxing Zeng

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

Mengtan DuDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, People's Republic of China.
Chenke DengDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, People's Republic of China.
Ting YuDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, People's Republic of China.
Qixin ZhouDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, People's Republic of China.
Fuxing ZengDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, No. 1088 Xueyuan Avenue, Shenzhen 518055, People's Republic of China.ORCID 0000-0003-0790-0151

Funding

Guangdong Basic and Applied Basic Research Foundation 2021A1515010805Guangdong Innovative and Entrepreneurial Research Team Program 2021ZT09Y104Guangdong Program 2021QN02Y353National Natural Science Foundation of China 32171200Shenzhen Science and Technology Program JCYJ20220530115210023
6 · The paper itself

Abstract

Ribosome biogenesis is a highly regulated cellular process that involves the control of numerous assembly factors. The small protein YjgA has been reported to play a role in the late stages of 50S assembly. However, the precise molecular mechanism underlying its function remains unclear. In this study, cryo-electron microscopy (cryo-EM) structures revealed that depletion of YjgA or its N-terminal loop in Escherichia coli both lead to the accumulation of immature 50S particles with structural abnormalities mainly in peptidyl transferase center (PTC) and H68/69 region. CryoDRGN analysis uncovered 8 and 6 distinct conformations of pre50S for ΔyjgA and YjgA-ΔNloop, respectively. These conformations highlighted the role of the N-terminal loop of YjgA in integrating uL16 and stabilizing H89 in PTC, which was further verified by the pull-down assays of YjgA and its mutants with uL16. Together with the function of undocking H68 through the binding of its C-terminal CTLH-like domain to the base of the L1 stalk, YjgA facilitates the maturation of PTC. This study identified critical domains of YjgA contributing to 50S assembly efficiency, providing a comprehensive understanding of the dual roles of YjgA in accelerating ribosome biogenesis and expanding our knowledge of the intricate processes governing cellular protein synthesis.

Indexed as

Cryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsModels, MolecularPeptidyl TransferasesProtein BindingRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialEscherichia coli ProteinsPeptidyl TransferasesRibosomal Proteins

Identifiers

PMID38842932
PMCPMC11260487

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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.