Purification and characterization of a novel and conserved TPR-domain protein that binds both Hsp90 and Hsp70 and is expressed in all developmental stages of Leishmania major

Araujo, Sara A.; Martins, Gustavo H.; Quel, Natália G.; Aragão, Annelize Zambon Barbosa; Morea, Edna Gicela Ortiz; Borges, Júlio César; Houry, Walid; Cano, Maria Isabel Nogueira; Ramos, Carlos H.I.

doi:10.1016/j.biochi.2020.12.017

Cited by 3 publications

(1 citation statement)

References 47 publications

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“…Notably, these values deviate from those expected for a non-hydrated sphere with a molecular mass equivalent to that of SbRPAP3, indicating that the protein possesses a non-globular shape. Specifically, the calculated Perrin factor of 1.65 suggests that SbRPAP3 adopts an elongated shape, which is characteristic of TPR-domain proteins [ 24 , 25 , 26 , 27 ].…”

Section: Resultsmentioning

confidence: 99%

Unveiling the Role of Sorghum RPAP3 in the Function of R2TP Complex: Insights into Protein Assembly in Plants

Antonio

Martins

Aragão

et al. 2023

Plants

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The chaperone R2TP has multiple subunits that assist in the proper folding, assembly, and stabilization of various protein complexes in cells and its study can offer valuable insights into the regulation and maintenance of protein assemblies in plant systems. The ‘T’ component of R2TP is Tah1 in yeast, consisting of 111 residues, while its counterpart in humans is RPAP3, with 665 residues. RPAP3 acts as a co-chaperone of Hsp90 and facilitates interactions between RUVBL proteins and other complex components, enhancing the recruitment of client proteins by the R2TP complex. These facts further underscore the relevance of studying this complex in different organisms. The putative gene corresponding to the RPAP3 in Sorghum bicolor, a monocotyledon plant, was cloned, and the protein (396 residues) purified for biochemical characterization. SbRPAP3 exists as a folded monomer and has a RPAP3 domain, which is present in human RPAP3 but absent in yeast Tah1. SbRPAP3 retains its functional capabilities, including binding with RUVBLs, Hsp90, and Hsp70. By elucidating the role of RPAP3 in plant R2TP complex, we can further comprehend the molecular mechanisms underlying plant-specific protein assembly and contribute to advancements in plant biology and biotechnological applications.

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Section: Resultsmentioning

confidence: 99%

Unveiling the Role of Sorghum RPAP3 in the Function of R2TP Complex: Insights into Protein Assembly in Plants

Antonio

Martins

Aragão

et al. 2023

Plants

Self Cite

View full text Add to dashboard Cite

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Therapeutic potential of ASK1 activators in cancer treatment: Current insights and future directions

Wang,

Ma,

Zhang

et al. 2024

Biomedicine & Pharmacotherapy

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Nuclear Hsp104 safeguards the dormant translation machinery during quiescence

Kohler,

Berglund

et al. 2024

Nat Commun

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The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.

show abstract

Purification and characterization of a novel and conserved TPR-domain protein that binds both Hsp90 and Hsp70 and is expressed in all developmental stages of Leishmania major

Cited by 3 publications

References 47 publications

Unveiling the Role of Sorghum RPAP3 in the Function of R2TP Complex: Insights into Protein Assembly in Plants

Unveiling the Role of Sorghum RPAP3 in the Function of R2TP Complex: Insights into Protein Assembly in Plants

Therapeutic potential of ASK1 activators in cancer treatment: Current insights and future directions

Nuclear Hsp104 safeguards the dormant translation machinery during quiescence

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