ArticleMolecular & cellular proteomics : MCP2017
Escherichia coli Proteome Microarrays Identified the Substrates of ClpYQ Protease.
Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
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- A Transient π-π or Cation-π Interaction between Degron and Degrader Dual Residues: A Key Step for the Substrate Recognition and Discrimination in the Processive Degradation of SulA by ClpYQ (HslUV) Protease inInternational journal of molecular sciences · 2023Article
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- Protein degradation control and regulation of bacterial survival and pathogenicity: the role of protein degradation systems in bacteria.Molecular biology reports · 2021Review
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Advances in Analysis of Milk Proteases Activity at Surfaces and in a Volume by Acoustic Methods.Sensors (Basel, Switzerland) · 2020Review
- Developments and Applications of Functional Protein Microarrays.Molecular & cellular proteomics : MCP · 2020Review
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
- Bacterial secretion chaperones: the mycobacterial type VII case.FEMS microbiology letters · 2018Review
- EspH is a hypervirulence factor for Mycobacterium marinum and essential for the secretion of the ESX-1 substrates EspE and EspF.PLoS pathogens · 2018Article
- Whole-cell biocatalysts by design.Microbial cell factories · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolysis is a vital mechanism to regulate the cellular proteome in all kingdoms of life, and ATP-dependent proteases play a crucial role within this process. In Escherichia coli, ClpYQ is one of the primary ATP-dependent proteases. In addition to function with removals of abnormal peptides in the cells, ClpYQ degrades regulatory proteins if necessary and thus let cells adjust to various environmental conditions. In E. coli, SulA, RcsA, RpoH and TraJ as well as RNase R, have been identified as natural protein substrates of ClpYQ. ClpYQ contains ClpY and ClpQ. The ATPase ClpY is responsible for protein recognition, unfolding, and translocation into the catalytic core of ClpQ. In this study, we use an indirect identification strategy to screen possible ClpY targets with E. coli K12 proteome chips. The chip assay results showed that YbaB strongly bound to ClpY. We used yeast two-hybrid assay to confirm the interactions between ClpY and YbaB protein and determined the K
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