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dc.contributor.author
Moreno Cabezuelo, José Ángel
dc.contributor.author
del Carmen Muñoz Marín, María
dc.contributor.author
López Lozano, Antonio
dc.contributor.author
Athayde, Diogo
dc.contributor.author
Simón García, Ana
dc.contributor.author
Díez, Jesús
dc.contributor.author
Archer, Margarida
dc.contributor.author
Issoglio, Federico Matías
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dc.contributor.author
García Fernández, José Manuel
dc.date.available
2024-02-27T11:26:39Z
dc.date.issued
2023-04
dc.identifier.citation
Moreno Cabezuelo, José Ángel; del Carmen Muñoz Marín, María; López Lozano, Antonio; Athayde, Diogo; Simón García, Ana; et al.; Production, homology modeling and mutagenesis studies on GlcH glucose transporter from Prochlorococcus sp. strain SS120; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1864; 2; 4-2023; 1-11
dc.identifier.issn
0005-2728
dc.identifier.uri
http://hdl.handle.net/11336/228511
dc.description.abstract
The marine cyanobacterium Prochlorococcus is one of the main primary producers on Earth, which can take up glucose by using the high affinity, multiphasic transporter GlcH. We report here the overexpression of glcH from Prochlorococcus marinus strain SS120 in Escherichia coli. Modeling studies of GlcH using the homologous MelB melibiose transporter from Salmonella enterica serovar Typhimurium showed high conservation at the overall fold. We observed that an important structural interaction, mediated by a strong hydrogen bond between D8 and R141, is conserved in Prochlorococcus, although the corresponding amino acids in MelB from Salmonella are different. Biased docking studies suggested that when glucose reaches the pocket of the transporter and interacts with D8 and R141, the hydrogen bond network in which these residues are involved could be disrupted, favoring a conformational change with the subsequent translocation of the glucose molecule towards the cytoplasmic region of the pmGlcH structure. Based on these theoretical predictions and on the conservation of N117 and W348 in other MelB structures, D8, N117, R141 and W348 were mutated to glycine residues. Their key role in glucose transport was evaluated by glucose uptake assays. N117G and W348G mutations led to 17 % decrease in glucose uptake, while D8G and R141G decreased the glucose transport by 66 % and 92 % respectively. Overall, our studies provide insights into the Prochlorococcus 3D-structure of GlcH, paving the way for further analysis to understand the features which are involved in the high affinity and multiphasic kinetics of this transporter.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
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dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CYANOBACTERIA
dc.subject
GLUCOSE
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HOMOLOGY MODELING
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MEMBRANE PROTEIN
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TRANSPORT
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Production, homology modeling and mutagenesis studies on GlcH glucose transporter from Prochlorococcus sp. strain SS120
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-02-26T11:11:11Z
dc.journal.volume
1864
dc.journal.number
2
dc.journal.pagination
1-11
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Moreno Cabezuelo, José Ángel. Universidad de Córdoba; España
dc.description.fil
Fil: del Carmen Muñoz Marín, María. Universidad de Córdoba; España
dc.description.fil
Fil: López Lozano, Antonio. Universidad de Córdoba; España
dc.description.fil
Fil: Athayde, Diogo. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Simón García, Ana. Universidad de Córdoba; España
dc.description.fil
Fil: Díez, Jesús. Universidad de Córdoba; España
dc.description.fil
Fil: Archer, Margarida. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Issoglio, Federico Matías. Universidade Nova de Lisboa; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: García Fernández, José Manuel. Universidad de Córdoba; España
dc.journal.title
Biochimica Et Biophysica Acta-bioenergetics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbabio.2022.148954
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005272822004248
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