ArticleThe Journal of biological chemistry2013
In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-cross-linker.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 56 citations in OpenAlex.
- A microaerobically induced small heat shock protein contributes toApplied and environmental microbiology · 2025Article
- Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Nature communications · 2021Article
- IbpB-bound substrate release in living cells as revealed by unnatural amino acid-mediated photo-crosslinking.FEBS open bio · 2020Article
- Structural and functional properties of proteins interacting with small heat shock proteins.Cell stress & chaperones · 2020Review
- Small but mighty: a functional look at bacterial sHSPs.Cell stress & chaperones · 2020Review
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- Chaperone-like activity of the N-terminal region of a human small heat shock protein and chaperone-functionalized nanoparticles.Proteins · 2019Article
- Broad range of missense error frequencies in cellular proteins.Nucleic acids research · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- Regrowth-delay body as a bacterial subcellular structure marking multidrug-tolerant persisters.Cell discovery · 2019Article
- Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau.Nature communications · 2018Article
- Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis.Cell stress & chaperones · 2018Article
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- Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii.Plant molecular biology · 2017Article
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- A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Journal of molecular biology · 2015Review
- A novel mechanism for small heat shock proteins to function as molecular chaperones.Scientific reports · 2015Article
- Protein plasticity underlines activation and function of ATP-independent chaperones.Frontiers in molecular biosciences · 2015Review
- A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrity.Journal of bacteriology · 2014Article
- Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins.Protein science : a publication of the Protein Society · 2014Article
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
Small heat shock proteins (sHSPs), as ubiquitous molecular chaperones found in all forms of life, are known to be able to protect cells against stresses and suppress the aggregation of a variety of model substrate proteins under in vitro conditions. Nevertheless, it is poorly understood what natural substrate proteins are protected by sHSPs in living cells. Here, by using a genetically incorporated photo-cross-linker (p-benzoyl-l-phenylalanine), we identified a total of 95 and 54 natural substrate proteins of IbpB (an sHSP from Escherichia coli) in living cells with and without heat shock, respectively. Functional profiling of these proteins (110 in total) suggests that IbpB, although binding to a wide range of cellular proteins, has a remarkable substrate preference for translation-related proteins (e.g. ribosomal proteins and amino-acyl tRNA synthetases) and moderate preference for metabolic enzymes. Furthermore, these two classes of proteins were found to be more prone to aggregation and/or inactivation in cells lacking IbpB under stress conditions (e.g. heat shock). Together, our in vivo data offer novel insights into the chaperone function of IbpB, or sHSPs in general, and suggest that the preferential protection on the protein synthesis machine and metabolic enzymes may dominantly contribute to the well known protective effect of sHSPs on cell survival against stresses.
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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.