The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway

Gaur, Deepika; Singh, Prashant; Guleria, Jyoti; Gupta, A. P.; Kaur, Satinderdeep; Sharma, Deepak

doi:10.1534/genetics.120.303190

Cited by 13 publications

(29 citation statements)

References 57 publications

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“…Thus, the presence of specific JDPs determines the fate of specific target substrates. Accordingly, a yeast-based study recently showed how the HSP70 homologue Ssa2 has significantly larger affinity for Ydj1 than its paralogue Ssa4, which may be the reason for the pronounced ability of Ssa2 to assist maturation of Hsp90 substrates [161]. Since JDPs regulate which substrates are presented to HSP70, they are essential components of the chaperone network.…”

Section: Regulation Of Chaperone Activitymentioning

confidence: 99%

Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome

et al. 2020

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Protein homeostasis (proteostasis) is essential for the cell and is maintained by a highly conserved protein quality control (PQC) system, which triages newly synthesized, mislocalized and misfolded proteins. The ubiquitin-proteasome system (UPS), molecular chaperones, and co-chaperones are vital PQC elements that work together to facilitate degradation of misfolded and toxic protein species through the 26S proteasome. However, the underlying mechanisms are complex and remain partly unclear. Here, we provide an overview of the current knowledge on the co-chaperones that directly take part in targeting and delivery of PQC substrates for degradation. While J-domain proteins (JDPs) target substrates for the heat shock protein 70 (HSP70) chaperones, nucleotide-exchange factors (NEFs) deliver HSP70-bound substrates to the proteasome. So far, three NEFs have been established in proteasomal delivery: HSP110 and the ubiquitin-like (UBL) domain proteins BAG-1 and BAG-6, the latter acting as a chaperone itself and carrying its substrates directly to the proteasome. A better understanding of the individual delivery pathways will improve our ability to regulate the triage, and thus regulate the fate of aberrant proteins involved in cell stress and disease, examples of which are given throughout the review.

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Section: Regulation Of Chaperone Activitymentioning

confidence: 99%

Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome

et al. 2020

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“…Ssa1p is a chaperon in the cytoplasm, involved in the protein folding and trafficking [47]. Ydj1p is a cochaperone protein of Ssa1p and participates in the activity of Ssa1p [48]. At present, there are still no reports on their applications in improving protein folding.…”

Section: The Effects Of Chaperones On Pinene Productionmentioning

confidence: 99%

Improved pinene production in a recombinant yeast by fusion linker optimization and chaperon coexpression

Ren

et al. 2021

Syst Microbiol and Biomanuf

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Pinene is an active natural monoterpene from plants and has important applications in flavorings, fragrances,and pesticides. Especially, pinene dimers are regarded as renewable fuels with high density. However, the microbial pinene production was limited by the low activity pinene synthase. In this study, the pinene synthase activity was improved by fusion linker optimization and chaperon coexpression. To construct the pinene pathway in Saccharomyces cerevisiae, YPL062W gene was deleted to increase the MVA pathway precursor acetyl-CoA. Truncated 3-hydroxyl-3-methylglutaryl-CoA reductase (tHMG1), isopentenyl-diphosphate isomerase (IDI1), and farnesyl diphosphate synthase mutant (ERG20 F96W−N127W ) were then integrated to improve the GPP pool. Pinene synthase tPt1 was expressed in the constructed engineered yeast, and the titer of pinene reached 0.166 mg/L. GPP is the direct precursor of pinene, ERG20 ww and tPt1 were fused by different linkers and orders to improve the accessibility of GPP. Pinene titer reached 9.94 mg/L by fusion these proteins in the order of ERG20 ww and tPt1 and with a flexible linker (G) 8 . After that, several chaperons were coexpressed and the chaperon Sil1p improved the pinene titer to 10.2 mg/L with a yield of 1.63 mg/L•OD 600 . The results presented here provide novel information on the applications of protein fusion and protein chaperons in microbial pinene production.

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“…Studies in yeast and mammals indicate that Hsp40s bind upstream of Hsp70s modulating their specificity [ 89 , 90 ]. In yeast, cytosolic Hsp40 chaperones such as Sis1, Xdj1, and Ydj1 were shown to recognize mitochondrial precursors and assist recruitment of Hsp70 (Ssa) chaperones [ 79 , 80 , 91 , 92 , 93 , 94 ].…”

Section: Molecular Chaperones Are Essential To Run the Post-translational Importmentioning

confidence: 99%

“…Multiple studies demonstrated the importance of the most abundant yeast Hsp40 Ydj1 as a docking agent for mitochondrial-targeted proteins [ 80 , 91 , 92 , 93 ]. The YDJ1 gene deletion affects both mitochondrial and ER targeting, causing severe growth defects [ 80 ].…”

Section: Molecular Chaperones Are Essential To Run the Post-translational Importmentioning

confidence: 99%

Cytosolic Quality Control of Mitochondrial Protein Precursors—The Early Stages of the Organelle Biogenesis

Lenkiewicz

Krakowczyk

Brągoszewski

2021

IJMS

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With few exceptions, proteins that constitute the proteome of mitochondria originate outside of this organelle in precursor forms. Such protein precursors follow dedicated transportation paths to reach specific parts of mitochondria, where they complete their maturation and perform their functions. Mitochondrial precursor targeting and import pathways are essential to maintain proper mitochondrial function and cell survival, thus are tightly controlled at each stage. Mechanisms that sustain protein homeostasis of the cytosol play a vital role in the quality control of proteins targeted to the organelle. Starting from their synthesis, precursors are constantly chaperoned and guided to reduce the risk of premature folding, erroneous interactions, or protein damage. The ubiquitin-proteasome system provides proteolytic control that is not restricted to defective proteins but also regulates the supply of precursors to the organelle. Recent discoveries provide evidence that stress caused by the mislocalization of mitochondrial proteins may contribute to disease development. Precursors are not only subject to regulation but also modulate cytosolic machinery. Here we provide an overview of the cellular pathways that are involved in precursor maintenance and guidance at the early cytosolic stages of mitochondrial biogenesis. Moreover, we follow the circumstances in which mitochondrial protein import deregulation disturbs the cellular balance, carefully looking for rescue paths that can restore proteostasis.

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The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway

Cited by 13 publications

References 57 publications

Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome

Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome

Improved pinene production in a recombinant yeast by fusion linker optimization and chaperon coexpression

Cytosolic Quality Control of Mitochondrial Protein Precursors—The Early Stages of the Organelle Biogenesis

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