The roles of molecular chaperones in regulating cell metabolism

Binder, M.; Pedley, Anthony M.

doi:10.1002/1873-3468.14682

Cited by 5 publications

(2 citation statements)

References 223 publications

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“…The participation of Hsp90 and Hsp70 chaperone families on human metabolic enzymes espetially their participation in enzymatic activities as participating in translocation and degradation of methabolic enzymes highlights their participation in disease-related disorders [ 62 ].…”

Section: Discussionmentioning

confidence: 99%

Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone

Roterman,

Stapor,

Konieczny

2023

BMC Bioinformatics

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Background The aqueous environment directs the protein folding process towards the generation of micelle-type structures, which results in the exposure of hydrophilic residues on the surface (polarity) and the concentration of hydrophobic residues in the center (hydrophobic core). Obtaining a structure without a hydrophobic core requires a different type of external force field than those generated by a water. The examples are membrane proteins, where the distribution of hydrophobicity is opposite to that of water-soluble proteins. Apart from these two extreme examples, the process of protein folding can be directed by chaperones, resulting in a structure devoid of a hydrophobic core. Results The current work presents such example: DnaJ Hsp40 in complex with alkaline phosphatase PhoA-U (PDB ID—6PSI)—the client molecule. The availability of WT form of the folding protein—alkaline phosphatase (PDB ID—1EW8) enables a comparative analysis of the structures: at the stage of interaction with the chaperone and the final, folded structure of this biologically active protein. The fuzzy oil drop model in its modified FOD-M version was used in this analysis, taking into account the influence of an external force field, in this case coming from a chaperone. Conclusions The FOD-M model identifies the external force field introduced by chaperon influencing the folding proces. The identified specific external force field can be applied in Ab Initio protein structure prediction as the environmental conditioning the folding proces.

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Section: Discussionmentioning

confidence: 99%

Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone

Roterman,

Stapor,

Konieczny

2023

BMC Bioinformatics

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“…Methenyltetrahydrofolate synthetase (MTHFS, EC 6.3.3.2), an enzyme catalyzing the ATP-dependent formation of cofactor 5,10-methenyltetrahydrofolate used by TrifGART and ATIC was shown to colocalize with two tested enzymes of the purinosome, TrifGART and FGAMS ( Field et al, 2011 ). Chaperones and co-chaperones from the Hsp70/Hsp90 system were also validated to regulate the formation of the purinosome ( Figure 7 ) by directly interacting with PPAT and FGAMS ( Binder and Pedley, 2013 ; French et al, 2013 ; Pedley et al, 2018 ).…”

Section: Navigating the Complexities Of Metabolon Formation For Finer...mentioning

confidence: 98%

A journey into the regulatory secrets of the de novo purine nucleotide biosynthesis

Ayoub,

Gedeon,

Munier-Lehmann

2024

Front. Pharmacol.

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De novo purine nucleotide biosynthesis (DNPNB) consists of sequential reactions that are majorly conserved in living organisms. Several regulation events take place to maintain physiological concentrations of adenylate and guanylate nucleotides in cells and to fine-tune the production of purine nucleotides in response to changing cellular demands. Recent years have seen a renewed interest in the DNPNB enzymes, with some being highlighted as promising targets for therapeutic molecules. Herein, a review of two newly revealed modes of regulation of the DNPNB pathway has been carried out: i) the unprecedent allosteric regulation of one of the limiting enzymes of the pathway named inosine 5′-monophosphate dehydrogenase (IMPDH), and ii) the supramolecular assembly of DNPNB enzymes. Moreover, recent advances that revealed the therapeutic potential of DNPNB enzymes in bacteria could open the road for the pharmacological development of novel antibiotics.

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The components of the AhR‐molecular chaperone complex differ depending on whether the ligands are toxic or non‐toxic

Narita,

Tamura,

Hatakeyama

et al. 2024

FEBS Letters

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The aryl hydrocarbon receptor (AhR) forms a complex with the HSP90‐XAP2‐p23 molecular chaperone when the cells are exposed to toxic compounds. Recently, 1,4‐dihydroxy‐2‐naphthoic acid (DHNA) was reported to be an AhR ligand. Here, we investigated the components of the molecular chaperone complex when DHNA binds to AhR. Proteins eluted from the 3‐Methylcolanthrene‐affinity column were AhR‐HSP90‐XAP2‐p23 complex. The AhR‐molecular chaperone complex did not contain p23 in the eluents from the DHNA‐affinity column. In 3‐MC‐treated cells, AhR formed a complex with HSP90‐XAP2‐p23 and nuclear translocation occurred within 30 min, while in DHNA‐treated cells, AhR formed a complex with AhR‐HSP90‐XAP2, and translocation was slow from 60 min. Thus, the AhR activation mechanism may differ when DHNA is the ligand compared to toxic ligands.

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The roles of molecular chaperones in regulating cell metabolism

Cited by 5 publications

References 223 publications

Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone

Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone

A journey into the regulatory secrets of the de novo purine nucleotide biosynthesis

The components of the AhR‐molecular chaperone complex differ depending on whether the ligands are toxic or non‐toxic

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