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  1. Article ; Online: 1

    Pellizza, Leonardo / Ramis, Lila / Araoz, Ignacio Argañaraz / Aran, Martín

    Biomolecular NMR assignments

    2023  Volume 17, Issue 2, Page(s) 229–233

    Abstract: The InterPro family IPR007621 TPM_phosphatase is a widely conserved family of protein domains found in prokaryotes, plants and invertebrates. Despite similar predicted protein folding, members of this family are involved in different cellular processes. ... ...

    Abstract The InterPro family IPR007621 TPM_phosphatase is a widely conserved family of protein domains found in prokaryotes, plants and invertebrates. Despite similar predicted protein folding, members of this family are involved in different cellular processes. In recent years, the structural and biochemical characterization of evolutionarily divergent TPM domains has shown their ability to hydrolyze phosphate groups of different substrates. However, there are still inaccurate functional annotations and uncertain relationships between the structure and function of this domain family. We here report the
    MeSH term(s) Nuclear Magnetic Resonance, Biomolecular ; Magnetic Resonance Spectroscopy ; Rhodothermus ; Protein Domains
    Language English
    Publishing date 2023-08-05
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-023-10146-2
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  2. Article: MliR, a novel MerR-like regulator of iron homeostasis, impacts metabolism, membrane remodeling, and cell adhesion in the marine Bacteroidetes

    Pellizza, Leonardo / Bialer, Magalí G / Sieira, Rodrigo / Aran, Martín

    Frontiers in microbiology

    2022  Volume 13, Page(s) 987756

    Abstract: The MerR family is a group of transcriptional activators with conserved N-terminal helix-turn-helix DNA binding domains and variable C-terminal effector binding regions. In most MerR proteins the effector binding domain (EBD) contains a cysteine center ... ...

    Abstract The MerR family is a group of transcriptional activators with conserved N-terminal helix-turn-helix DNA binding domains and variable C-terminal effector binding regions. In most MerR proteins the effector binding domain (EBD) contains a cysteine center suited for metal binding and mediates the response to environmental stimuli, such as oxidative stress, heavy metals or antibiotics. We here present a novel transcriptional regulator classified in the MerR superfamily that lacks an EBD domain and has neither conserved metal binding sites nor cysteine residues. This regulator from the psychrotolerant bacteria
    Language English
    Publishing date 2022-09-02
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2022.987756
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  3. Article ; Online: Gcn4 impacts metabolic fluxes to promote yeast chronological lifespan.

    Gulias, Juan Facundo / Niesi, Florencia / Arán, Martín / Correa-García, Susana / Bermúdez-Moretti, Mariana

    PloS one

    2023  Volume 18, Issue 10, Page(s) e0292949

    Abstract: Aging is characterized by a gradual decline in physiological integrity, which impairs functionality and increases susceptibility to mortality. Dietary restriction, mimicking nutrient scarcity without causing malnutrition, is an intervention known to ... ...

    Abstract Aging is characterized by a gradual decline in physiological integrity, which impairs functionality and increases susceptibility to mortality. Dietary restriction, mimicking nutrient scarcity without causing malnutrition, is an intervention known to decelerate the aging process. While various hypotheses have been proposed to elucidate how dietary restriction influences aging, the underlying mechanisms remain incompletely understood. This project aimed to investigate the role of the primary regulator of the general amino acid control (GAAC) pathway, the transcription factor Gcn4, in the aging process of S. cerevisiae cells. Under conditions of amino acid deprivation, which activate Gcn4, the deletion of GCN4 led to a diverse array of physiological changes in the cells. Notably, the absence of Gcn4 resulted in heightened mitochondrial activity, likely contributing to the observed increase in reactive oxygen species (ROS) accumulation. Furthermore, these mutant gcn4Δ cells exhibited reduced ethanol production despite maintaining similar glucose consumption rates, suggesting a pivotal role for Gcn4 in regulating the Crabtree effect. Additionally, there was a marked reduction in trehalose, the storage carbohydrate, within the mutant cells compared to the wild-type strain. The intracellular content of free amino acids also exhibited disparities between the wild-type and GCN4-deficient strains. Taken together, our findings indicate that the absence of GCN4 disrupts cellular homeostasis, triggering significant alterations in interconnected intracellular metabolic pathways. These disruptions have far-reaching metabolic consequences that ultimately culminate in a shortened lifespan.
    MeSH term(s) Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Longevity ; Protein Biosynthesis ; Amino Acids/metabolism ; Gene Expression Regulation, Fungal ; Fungal Proteins/genetics
    Chemical Substances Saccharomyces cerevisiae Proteins ; Amino Acids ; Fungal Proteins
    Language English
    Publishing date 2023-10-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0292949
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  4. Article ; Online: Cadmium and copper-induced metabolic and proteomic changes in the root tip during early maize growth.

    Matayoshi, Carolina Lucila / Jiménez Guaman, Odalis Maholi / Esteso, Marcos Leopoldo / Pavoni, Micaela / Arán, Martín / Pena, Liliana Beatriz / Gallego, Susana Mabel

    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine

    2023  Volume 37, Issue 2, Page(s) 405–419

    Abstract: In this study, the metabolic adjustments performed by maize (Zea mays L.) seminal roots exposed to 25 µM ... ...

    Abstract In this study, the metabolic adjustments performed by maize (Zea mays L.) seminal roots exposed to 25 µM Cd
    MeSH term(s) Copper/metabolism ; Cadmium/metabolism ; Zea mays/metabolism ; Meristem/metabolism ; Hydrogen Peroxide/metabolism ; Proteomics ; Plant Roots/metabolism ; Soil Pollutants/metabolism
    Chemical Substances Copper (789U1901C5) ; Cadmium (00BH33GNGH) ; Hydrogen Peroxide (BBX060AN9V) ; Soil Pollutants
    Language English
    Publishing date 2023-11-21
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1112688-7
    ISSN 1572-8773 ; 0966-0844
    ISSN (online) 1572-8773
    ISSN 0966-0844
    DOI 10.1007/s10534-023-00557-y
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2515: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Book: Nocturno en el Mery's bar

    Arán, Martín

    (Colección Los días terrestres : Narrativa ; 21)

    2012  

    Author's details Martín Arán
    Series title Colección Los días terrestres : Narrativa ; 21
    Language Spanish
    Size 278 p, 20 cm
    Publisher E.D.A Libros
    Publishing place Benalmádena
    Document type Book
    Note Novel
    ISBN 9788492821464 ; 8492821469
    Database Former special subject collection: coastal and deep sea fishing

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  6. Article ; Online: Codon usage clusters correlation: towards protein solubility prediction in heterologous expression systems in E. coli.

    Pellizza, Leonardo / Smal, Clara / Rodrigo, Guido / Arán, Martín

    Scientific reports

    2018  Volume 8, Issue 1, Page(s) 10618

    Abstract: Production of soluble recombinant proteins is crucial to the development of industry and basic research. However, the aggregation due to the incorrect folding of the nascent polypeptides is still a mayor bottleneck. Understanding the factors governing ... ...

    Abstract Production of soluble recombinant proteins is crucial to the development of industry and basic research. However, the aggregation due to the incorrect folding of the nascent polypeptides is still a mayor bottleneck. Understanding the factors governing protein solubility is important to grasp the underlying mechanisms and improve the design of recombinant proteins. Here we show a quantitative study of the expression and solubility of a set of proteins from Bizionia argentinensis. Through the analysis of different features known to modulate protein production, we defined two parameters based on the %MinMax algorithm to compare codon usage clusters between the host and the target genes. We demonstrate that the absolute difference between all %MinMax frequencies of the host and the target gene is significantly negatively correlated with protein expression levels. But most importantly, a strong positive correlation between solubility and the degree of conservation of codons usage clusters is observed for two independent datasets. Moreover, we evince that this correlation is higher in codon usage clusters involved in less compact protein secondary structure regions. Our results provide important tools for protein design and support the notion that codon usage may dictate translation rate and modulate co-translational folding.
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Codon ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Flavobacteriaceae/genetics ; Flavobacteriaceae/metabolism ; Protein Biosynthesis/genetics ; Protein Structure, Secondary/genetics ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Solubility
    Chemical Substances Bacterial Proteins ; Codon ; Recombinant Proteins
    Language English
    Publishing date 2018-07-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-018-29035-z
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  7. Article ; Online: Remodelling the surface of thioredoxin from

    Vazquez, Diego S / Agudelo, William A / Ferrer-Sueta, Gerardo / Giraudo, Laura / González Lebrero, Mariano C / Aran, Martín / Santos, Javier

    Dalton transactions (Cambridge, England : 2003)

    2022  Volume 51, Issue 46, Page(s) 17587–17601

    Abstract: In this work, we have designed and generated a Fe(III)-binding protein with thiol oxidoreductase activity. The consensus iron-binding motif EExxED from the frataxin protein family was grafted on a model peptide and on the surface of thioredoxin (TRX) ... ...

    Abstract In this work, we have designed and generated a Fe(III)-binding protein with thiol oxidoreductase activity. The consensus iron-binding motif EExxED from the frataxin protein family was grafted on a model peptide and on the surface of thioredoxin (TRX) from
    MeSH term(s) Escherichia coli/chemistry ; Iron/chemistry ; Escherichia coli Proteins/chemistry ; Binding Sites ; Thioredoxins/chemistry ; Thioredoxins/metabolism ; Sulfhydryl Compounds/chemistry ; Oxidoreductases/metabolism
    Chemical Substances Iron (E1UOL152H7) ; Escherichia coli Proteins ; Thioredoxins (52500-60-4) ; Sulfhydryl Compounds ; Oxidoreductases (EC 1.-)
    Language English
    Publishing date 2022-11-29
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472887-4
    ISSN 1477-9234 ; 1364-5447 ; 0300-9246 ; 1477-9226
    ISSN (online) 1477-9234 ; 1364-5447
    ISSN 0300-9246 ; 1477-9226
    DOI 10.1039/d2dt02599j
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  8. Article ; Online: Selection of synthetic proteins to modulate the human frataxin function.

    Pignataro, María Florencia / Herrera, María Georgina / Fernández, Natalia Brenda / Aran, Martín / Gentili, Hernán Gustavo / Battaglini, Fernando / Santos, Javier

    Biotechnology and bioengineering

    2022  Volume 120, Issue 2, Page(s) 409–425

    Abstract: Frataxin is a kinetic activator of the mitochondrial supercomplex for iron-sulfur cluster assembly. Low frataxin expression or a decrease in its functionality results in Friedreich's Ataxia (FRDA). With the aim of creating new molecular tools to study ... ...

    Abstract Frataxin is a kinetic activator of the mitochondrial supercomplex for iron-sulfur cluster assembly. Low frataxin expression or a decrease in its functionality results in Friedreich's Ataxia (FRDA). With the aim of creating new molecular tools to study this metabolic pathway, and ultimately, to explore new therapeutic strategies, we have investigated the possibility of obtaining small proteins exhibiting a high affinity for frataxin. In this study, we applied the ribosome display approach, using human frataxin as the target. We focused on Affi_224, one of the proteins that we were able to select after five rounds of selection. We have studied the interaction between both proteins and discussed some applications of this specific molecular tutor, concerning the modulation of the supercomplex activity. Affi_224 and frataxin showed a K
    MeSH term(s) Humans ; Iron-Binding Proteins/genetics ; Iron-Binding Proteins/chemistry ; Iron-Binding Proteins/metabolism ; Carbon-Sulfur Lyases/chemistry ; Carbon-Sulfur Lyases/metabolism ; Frataxin
    Chemical Substances Iron-Binding Proteins ; NFS1 protein, human (EC 4.4.1.-) ; Carbon-Sulfur Lyases (EC 4.4.-)
    Language English
    Publishing date 2022-10-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.28263
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    In stock of ZB MED Cologne/Königswinter

    Zs.B 960: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  9. Article ; Online: Molten Globule Driven and Self-downmodulated Phase Separation of a Viral Factory Scaffold

    Salgueiro, Mariano / Camporeale, Gabriela / Visentin, Araceli / Arán, Martín / Pellizza, Leonardo / Esperante, Sebastián A. / Corbat, Agustín / Grecco, Hernán / Sousa, Belén / Esperón, Ramiro / Borkosky, Silvia S. / de Prat-Gay, Gonzalo

    Journal of Molecular Biology. 2023 May 18, p.168153-

    2023  , Page(s) 168153–

    Abstract: Viral factories of liquid-like nature serve as sites for transcription and replication in most viruses. The respiratory syncytial virus factories include replication proteins, brought together by the phosphoprotein (P) RNA polymerase cofactor, present ... ...

    Abstract Viral factories of liquid-like nature serve as sites for transcription and replication in most viruses. The respiratory syncytial virus factories include replication proteins, brought together by the phosphoprotein (P) RNA polymerase cofactor, present across non-segmented negative stranded RNA viruses. Homotypic liquid–liquid phase separation of RSV-P is governed by an α-helical molten globule domain, and strongly self-downmodulated by adjacent sequences. Condensation of P with the nucleoprotein N is stoichiometrically tuned, defining aggregate-droplet and droplet-dissolution boundaries. Time course analysis show small N-P nuclei gradually coalescing into large granules in transfected cells. This behavior is recapitulated in infection, with small puncta evolving to large viral factories, strongly suggesting that P-N nucleation-condensation sequentially drives viral factories. Thus, the tendency of P to undergo phase separation is moderate and latent in the full-length protein but unleashed in the presence of N or when neighboring disordered sequences are deleted. This, together with its capacity to rescue nucleoprotein-RNA aggregates suggests a role as a “solvent-protein”.
    Keywords DNA-directed RNA polymerase ; RNA ; Respiratory syncytial virus ; molecular biology ; nucleoproteins ; phosphoproteins ; separation ; RSV ; phosphoprotein ; molten globule ; viral factory ; LLPS
    Language English
    Dates of publication 2023-0518
    Publishing place Elsevier Ltd
    Document type Article ; Online
    Note Pre-press version
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2023.168153
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 4' 63/108: Show issues

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  10. Article ; Online: Direct Cysteine Desulfurase Activity Determination by NMR and the Study of the Functional Role of Key Structural Elements of Human NFS1.

    Sewell, Karl E / Gola, Gabriel F / Pignataro, María Florencia / Herrera, María Georgina / Noguera, Martín E / Olmos, Justo / Ramírez, Javier A / Capece, Luciana / Aran, Martín / Santos, Javier

    ACS chemical biology

    2023  Volume 18, Issue 7, Page(s) 1534–1547

    Abstract: The mitochondrial cysteine desulfurase NFS1 is an essential PLP-dependent enzyme involved in iron-sulfur cluster assembly. The enzyme catalyzes the desulfurization of the l-Cys substrate, producing a persulfide and l-Ala as products. In this study, we ... ...

    Abstract The mitochondrial cysteine desulfurase NFS1 is an essential PLP-dependent enzyme involved in iron-sulfur cluster assembly. The enzyme catalyzes the desulfurization of the l-Cys substrate, producing a persulfide and l-Ala as products. In this study, we set the measurement of the product l-Ala by NMR in vitro by means of
    MeSH term(s) Humans ; Iron-Sulfur Proteins/chemistry ; Carbon-Sulfur Lyases/metabolism ; Sulfur/chemistry ; Iron/chemistry ; Iron-Binding Proteins/chemistry ; Iron-Binding Proteins/genetics
    Chemical Substances cysteine desulfurase (EC 4.4.1.-) ; Iron-Sulfur Proteins ; Carbon-Sulfur Lyases (EC 4.4.-) ; Sulfur (70FD1KFU70) ; Iron (E1UOL152H7) ; Iron-Binding Proteins ; NFS1 protein, human (EC 4.4.1.-)
    Language English
    Publishing date 2023-07-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.3c00147
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