The protein scaffold calibrates metal specificity and activation in MerR sensors

Vista sencilla de ítem
dc.citation.titleMicrobial Biotechnology
dc.citation.volume15
dc.contributor.orcidhttps://orcid.org/0000-0002-1975-3606
dc.contributor.orcidhttps://orcid.org/0000-0002-8925-7763
dc.contributor.orcidhttps://orcid.org/0000-0003-1629-2848
dc.creatorMendoza, Julián I.
dc.creatorLescano, Julián
dc.creatorSoncini, Fernando C.
dc.creatorCheca, Susana Karina
dc.date.accessioned2024-05-14T16:08:21Z
dc.date.available2024-05-14T16:08:21Z
dc.date.issued2022
dc.description.abstractMerR metalloregulators are the central components of many biosensor plat-forms designed to report metal contamination. However, most MerR proteins are non-specific. This makes it difficult to apply these biosensors in the analy-sis of real environmental samples. On-demand implementation of molecular engineering to modify the MerR metal preferences is innovative, although it does not always yield the expected results. As the metal binding loop region (MBL) of these sensors has been proposed to be the major modulator of their specificity, we surgically switched this region for that of well-characterized specific and non-specific homologues. We found that identical modifications in different MerR proteins result in synthetic sensors displaying particular metal-detection patterns that cannot be predicted from the nature of the as-sembled modules. For instance, the MBL from a native Hg(II) sensor provided non-specificity or specificity toward Hg(II) or Cd(II) depending on the MerR scaffold into which it was integrated. These and other evidences reveal that residues outside the MBL are required to modulate ion recognition and trans-duce the input signal to the target promoter. Revealing their identity and their interactions with other residues is a critical step toward the design of more efficient biosensor devices for environmental metal monitoring.
dc.description.filFil: Mendoza, Julián. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.filFil: Lescano, Julián. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.filFil: Soncini, Fernando. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.filFil: Soncini, Fernando C. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Checa, Susana Karina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.filFil: Checa, Susana Karina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación (Agencia I+D+I): PICT‐2019‐00333
dc.format.extent2992-3002
dc.identifier.issn1751-7915
dc.identifier.urihttps://hdl.handle.net/2133/27038
dc.language.isoen
dc.publisherWiley Open Access
dc.relation.publisherversionhttps://enviromicro-journals.onlinelibrary.wiley.com/doi/epdf/10.1111/1751-7915.14151
dc.relation.publisherversionhttps://doi.org/10.1111/1751-7915.14151
dc.rightsopenAccess
dc.rights.holderMendoza, Julián I.
dc.rights.holderLescano, Julián
dc.rights.holderSoncini, Fernando C.
dc.rights.holderCheca, Susana Karina
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectBacterial proteins
dc.subjectDNA-binding proteins
dc.subjectMercury
dc.subjectMetals
dc.subjectPromoter regions
dc.titleThe protein scaffold calibrates metal specificity and activation in MerR sensors
dc.typearticulo
dc.type.versionpublishedVersion

Archivos

Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
The protein scaffold calibrates metal specificity and activation in MerR sensors.pdf
Tamaño:
4.29 MB
Formato:
Adobe Portable Document Format
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
Nombre:
license.txt
Tamaño:
3.87 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar

Colecciones

(FBIOyF) Departamento de Microbiología - Artículos