NAGIOS: RODERIC FUNCIONANDO

Identification and molecular characterization of the high-affinity copper transporters family in Solanum lycopersicum

Repositori DSpace/Manakin

IMPORTANT: Aquest repositori està en una versió antiga des del 3/12/2023. La nova instal.lació está en https://roderic.uv.es/

Identification and molecular characterization of the high-affinity copper transporters family in Solanum lycopersicum

Mostra el registre parcial de l'element

dc.contributor.author Romero, Paco
dc.contributor.author Gabrielli, Alessandro
dc.contributor.author Sampedro, Raúl
dc.contributor.author Perea García, Ana
dc.contributor.author Puig Todolí, Sergi
dc.contributor.author Lafuente Rodríguez, Mª Teresa
dc.date.accessioned 2022-05-18T12:31:10Z
dc.date.available 2022-05-18T12:31:10Z
dc.date.issued 2021
dc.identifier.citation Romero, Paco Gabrielli, Alessandro Sampedro, Raúl Perea García, Ana Puig Todolí, Sergi Lafuente Rodríguez, Mª Teresa 2021 Identification and molecular characterization of the high-affinity copper transporters family in Solanum lycopersicum International Journal of Biological Macromolecules 192 600 610
dc.identifier.uri https://hdl.handle.net/10550/82827
dc.description.abstract Copper (Cu) plays a key role as cofactor in the plant proteins participating in essential cellular processes, such as electron transport and free radical scavenging. Despite high-affinity Cu transporters (COPTs) being key participants in Cu homeostasis maintenance, very little is known about COPTs in tomato (Solanum lycopersicum) even though it is the most consumed fruit worldwide and this crop is susceptible to suboptimal Cu conditions. In this study, a six-member family of COPT (SlCOPT1-6) was identified and characterized. SlCOPTs have a conserved architecture consisting of three transmembrane domains and β-strains. However, the presence of essential methionine residues, a methionine-enriched amino-terminal region, an Mx3Mx12Gx3G Cu-binding motif and a cysteine rich carboxy-terminal region, all required for their functionality, is more variable among members. Accordingly, functional complementation assays in yeast indicate that SlCOPT1 and SlCOPT2 are able to transport Cu inside the cell, while SlCOPT3 and SlCOPT5 are only partially functional. In addition, protein interaction network analyses reveal the connection between SlCOPTs and Cu PIB-type ATPases, other metal transporters, and proteins related to the peroxisome. Gene expression analyses uncover organ-dependency, fruit vasculature tissue specialization and ripening-dependent gene expression profiles, as well as different response to Cu deficiency or toxicity in an organ-dependent manner.
dc.language.iso eng
dc.relation.ispartof International Journal of Biological Macromolecules, 2021, vol. 192, p. 600-610
dc.subject Tomàquets
dc.subject Biotecnologia agrícola
dc.title Identification and molecular characterization of the high-affinity copper transporters family in Solanum lycopersicum
dc.type journal article es_ES
dc.date.updated 2022-05-18T12:31:11Z
dc.identifier.doi 10.1016/j.ijbiomac.2021.10.032
dc.identifier.idgrec 153627
dc.rights.accessRights open access es_ES

Visualització       (5.133Mb)

Aquest element apareix en la col·lecció o col·leccions següent(s)

Mostra el registre parcial de l'element

Cerca a RODERIC

Cerca avançada

Visualitza

Estadístiques