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dc.contributor.author
Pedetta, Andrea
dc.contributor.author
Massazza, Diego Ariel
dc.contributor.author
Herrera Seitz, Karina
dc.contributor.author
Studdert, Claudia Alicia
dc.date.available
2018-11-27T13:38:01Z
dc.date.issued
2017-07
dc.identifier.citation
Pedetta, Andrea; Massazza, Diego Ariel; Herrera Seitz, Karina; Studdert, Claudia Alicia; Mutational Replacements at the "glycine Hinge" of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue; American Chemical Society; Biochemistry; 56; 29; 7-2017; 3850-3862
dc.identifier.issn
0006-2960
dc.identifier.uri
http://hdl.handle.net/11336/65271
dc.description.abstract
Bacterial chemoreceptors are dimeric membrane proteins that transmit signals from a periplasmic ligand-binding domain to the interior of the cells. The highly conserved cytoplasmic domain consists of a long hairpin that in the dimer forms a four-helix coiled-coil bundle. The central region of the bundle couples changes in helix packing that occur in the membrane proximal region to the signaling tip, controlling the activity of an associated histidine kinase. This subdomain contains certain glycine residues that are postulated to form a hinge in chemoreceptors from enteric bacteria and have been largely postulated to play a role in the coupling mechanism, and/or in the formation of higher-order chemoreceptor assemblies. In this work, we directly assessed the importance of the "glycine hinge" by obtaining nonfunctional replacements at each of its positions in the Escherichia coli serine receptor Tsr and characterizing them. Our results indicate that, rather than being essential for proper receptor-receptor interaction, the "glycine hinge" residues are involved in the ability of the receptor to switch between different signaling states. Mainly, the C-helix residue G439 has a key role in shifting the equilibrium toward a kinase-activating conformation. However, we found second-site mutations that restore the chemotactic proficiency of some of the "glycine hinge" mutants, suggesting that a complete hinge is not strictly essential. Rather, glycine residues seem to favor the coupling activity that relies on some other structural features of the central subdomain.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Bacterial Chemotaxis
dc.subject
Signal Transduction
dc.subject
Glycine Hinge
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Mutational Replacements at the "glycine Hinge" of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-10-23T14:10:37Z
dc.journal.volume
56
dc.journal.number
29
dc.journal.pagination
3850-3862
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Pedetta, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Massazza, Diego Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones en Ciencia y Tecnología de Materiales. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Instituto de Investigaciones en Ciencia y Tecnología de Materiales; Argentina
dc.description.fil
Fil: Herrera Seitz, Karina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Studdert, Claudia Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.journal.title
Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/acs.biochem.7b00455
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/acs.biochem.7b00455


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