Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability

Micheletto, Mariana C.; Mendes, Luis Felipe Santos; Basso, Luis G.M.; Fonseca-Maldonado, Raquel; Costa-Filho, Antonio J.

doi:10.1016/j.ijbiomac.2017.03.197

Cited by 13 publications

(10 citation statements)

References 41 publications

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“…This indicates that CnACBP preferentially binds anion membranes over neutral membranes. By exploring the effects of OCoA and phospholipids on the structure and stability of CnACBP, it is helpful to understand the process of CnACBP transport to different parts of cells after binding with lipids [65].…”

Section: The Function Of Acbp From C Neoformansmentioning

confidence: 99%

“…There are two ACBP family proteins in yeast S. carlsbergensis, among which ACBP type 1 exhibits a high binding affinity for palmitoyl-CoA [16]. Recently, a study using size exclusion chromatography (SEC) revealed that CnACBP from C. neoformans has a high binding affinity for oleoyl-COA and palmitoyl-COA, which can affect the spatial structure and stability of CnACBP [65] (Table 2). Table 1.…”

Section: The Binding Characteristics Of Acbp Family Proteins From Yeamentioning

confidence: 99%

“…It can improve acyl-CoA synthesis and regulates the production and degradation of intracellular NADPH [61] Cryptococcus neoformans Acb1 It is important for mating and filamentation, and preferentially binds to anion lipid membranes [64,65] Saccharomyces carlsbergensis ACBP type1/2 It can bind to acyl-CoA and improve the expansion of the intracellular acyl-CoA pool [16]…”

Section: Fungus Acbp Family Proteins Proposed Function Referencementioning

confidence: 99%

“…At present, most of the studies on ACBP family proteins in filamentous fungi are mainly focused on its functions in A. oryzae and M. ruber. However, the specific roles of the ACBP family proteins in lipid metabolism and their influence on the physiological functions of mycelium are rarely involved, and there is little related research on ACBP family proteins in other filamentous fungi [13,53,65,68]. There are two ACBP family proteins in A. oryzae.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

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Advances in Understanding the Acyl-CoA-Binding Protein in Plants, Mammals, Yeast, and Filamentous Fungi

Qiu

Zeng

2020

JoF

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Acyl-CoA-binding protein (ACBP) is an important protein with a size of about 10 kDa. It has a high binding affinity for C12–C22 acyl-CoA esters and participates in lipid metabolism. ACBP and its family of proteins have been found in all eukaryotes and some prokaryotes. Studies have described the function and structure of ACBP family proteins in mammals (such as humans and mice), plants (such as Oryza sativa, Arabidopsis thaliana, and Hevea brasiliensis) and yeast. However, little information on the structure and function of the proteins in filamentous fungi has been reported. This article concentrates on recent advances in the research of the ACBP family proteins in plants and mammals, especially in yeast, filamentous fungi (such as Monascus ruber and Aspergillus oryzae), and fungal pathogens (Aspergillus flavus, Cryptococcus neoformans). Furthermore, we discuss some problems in the field, summarize the binding characteristics of the ACBP family proteins in filamentous fungi and yeast, and consider the future of ACBP development.

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Section: The Function Of Acbp From C Neoformansmentioning

confidence: 99%

Section: The Binding Characteristics Of Acbp Family Proteins From Yeamentioning

confidence: 99%

Section: Fungus Acbp Family Proteins Proposed Function Referencementioning

confidence: 99%

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

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Advances in Understanding the Acyl-CoA-Binding Protein in Plants, Mammals, Yeast, and Filamentous Fungi

Qiu

Zeng

2020

JoF

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“…Todos os experimentos foram repetidos pelo menos duas vezes. A taxa de reversibilidade (%) é dada por: ΔHvH = 4R(Tmax) 2 Cp, max /ΔHcal onde R é a constante universal dos gases (1.987 cal K −1 mol −1 ), Tmax (= TM) é a temperatura absoluta, Cp,max é o valor máximo do excesso de capacidade de calor, e ΔHcal é a mudança de entalpia calorimétrica, calculada como a área abaixo do pico (MICHELETTO et al, 2017). A concentração das proteínas variou entre 2 e 4 mg/mL.…”

Section: Calorimetria Diferencial De Varreduraunclassified

Expressão, purificação e caracterização do domínio GOLD da proteína TMED 1 humana

Mota¹

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TMED proteins are eukaryotic transmembrane proteins present in all subcompartments of the early secretory pathway, i.e. the endoplasmic reticulum (ER), Golgi and the intermediate compartments. Although essential in the bidirectional protein transport between the ER and Golgi, TMEDs still lack information about their structure, oligomeric state and their interactions with the transport cargo. For the first time, the heterologous expression, biophysical characterization and the high-resolution structure of the human TMED1 GOLD domain are described. The recombinant protein was purified in two chromatographic steps, presenting a satisfactory yield and purity for the biophysical studies. The analysis of the circular dichroism data (CD) showed that, after purification, the protein was folded and that its secondary structure is predominantly composed of β-strands (~44%). The chemical denaturation of its secondary structures was monitored by CD in the region of the far ultraviolet. The protein was chemically stable, and the denaturation curve followed a sigmoid-like profile (cooperative) with a concentration of half transition of approximately 2.8 M urea. Tyrosine intrinsic fluorescence spectroscopy was also used to assess the stability in the presence of urea, resulting in a transition occurring at ca. 1.2 M. The protein presented high thermal stability with a melting temperature of about 60 °C and following a transition model of non-two-states, which indicated a probable dissociation of dimer to monomers to unfolded structures. DSF data showed that the ionicstrength was important for the structural stability of the GOLD domain. The protein was successfully crystallized, and its structure determined at a resolution of 1.7 Å. The 3D structure showed the traditional arrangement of the TMED GOLD domains, with a structural organization of a β-sandwich fold composed of two four-strand antiparallel β-sheets connected by a disulphide bond. The curvature of the molecule defines visually two different "sides" in this conformational organization called concave (formed by β2, β7, β4, and β5) and convex sides (formed by β6, β3, β8, and β1). We used the high-resolution structural model of the TMED1 GOLD dimer to perform molecular dynamic simulations, which showed that the dimer was energetically favorable and stable during the simulation time. Dimerization was favored by hydrogen bonds, hydrophobic interactions and π-π interactions. Studies to evaluate the formation of oligomers as a function of the concentration and ionic-strength suggest that the formation of dimers depended on both factors. Here, we propose a model for the anchoring of the dimer to the membrane based on the surface electrostatic charge of the protein. In such a model, the dimer is oriented with its convex side towards the cytosol, which is in accordance with the in vivo model previously reported and that would allow interaction with the ST2 receptor. The fact that the Golgi complex and the ER membranes are enriched in negativelycharged lipids gives potential func...

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The potential role of liquid–liquid phase separation in the cellular fate of the compartments for unconventional protein secretion

Mendes,

Gimenes,

da Silva

et al. 2024

Protein Science

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Eukaryotic cells have developed intricate mechanisms for biomolecule transport, particularly in stressful conditions. This interdisciplinary study delves into unconventional protein secretion (UPS) pathways activated during starvation, facilitating the export of proteins bypassing most of the components of the classical secretory machinery. Specifically, we focus on the underexplored mechanisms of the GRASP's role in UPS, particularly in biogenesis and cargo recruitment for the vesicular‐like compartment for UPS. Our results show that liquid–liquid phase separation (LLPS) plays a key role in the coacervation of Grh1, the GRASP yeast homologue, under starvation‐like conditions. This association seems a precursor to the Compartment for Unconventional Protein Secretion (CUPS) biogenesis. Grh1's self‐association is regulated by electrostatic, hydrophobic, and hydrogen‐bonding interactions. Importantly, our study demonstrates that phase‐separated states of Grh1 can recruit UPS cargo under starvation‐like situations. Additionally, we explore how the coacervate liquid‐to‐solid transition could impact cells' ability to return to normal post‐stress states. Our findings offer insights into intracellular protein dynamics and cell adaptive responses to stress.

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Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability

Cited by 13 publications

References 41 publications

Advances in Understanding the Acyl-CoA-Binding Protein in Plants, Mammals, Yeast, and Filamentous Fungi

Advances in Understanding the Acyl-CoA-Binding Protein in Plants, Mammals, Yeast, and Filamentous Fungi

Expressão, purificação e caracterização do domínio GOLD da proteína TMED 1 humana

The potential role of liquid–liquid phase separation in the cellular fate of the compartments for unconventional protein secretion

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