Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems
The ability to perceive the environment, an essential attribute in living organisms, is linked to the evolution of signalling proteins that recognize specific signals and execute predetermined responses. Such proteins constitute concerted systems that can be as simple as a unique protein, able to re...
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| Format: | bookPart |
| Sprog: | engelsk |
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2020
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| Online adgang: | https://hdl.handle.net/20.500.12381/602 |
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| _version_ | 1868890011474067456 |
|---|---|
| author | Trajtenberg, Felipe |
| author2 | Buschiazzo, Alejandro |
| author2_role | author |
| author_browse | Buschiazzo, Alejandro Trajtenberg, Felipe |
| author_facet | Trajtenberg, Felipe Buschiazzo, Alejandro |
| author_role | author |
| collection | IPMON en REDI |
| dc.creator.none.fl_str_mv | Trajtenberg, Felipe Buschiazzo, Alejandro |
| dc.date.none.fl_str_mv | 2020 2022-07-01T14:02:33Z 2022-07-01T14:02:33Z |
| dc.identifier.none.fl_str_mv | https://hdl.handle.net/20.500.12381/602 FCE_1_2017_1_136291 10.1007/978-1-4939-9884-5_1 |
| dc.language.none.fl_str_mv | eng |
| dc.publisher.none.fl_str_mv | Springer Nature (Humana Press) |
| dc.relation.none.fl_str_mv | https://hdl.handle.net/20.500.12381/603 https://hdl.handle.net/20.500.12381/604 |
| dc.rights.none.fl_str_mv | Acceso abierto info:eu-repo/semantics/openAccess Reconocimiento-NoComercial-SinObraDerivada 4.0 Internacional. (CC BY-NC-ND) |
| dc.source.none.fl_str_mv | Histidine Phosphorylation - Methods and Protocols reponame:IPMON en REDI instname:Institut Pasteur de Montevideo instacron:Institut Pasteur de Montevideo |
| dc.subject.none.fl_str_mv | señalización bacteriana Fosforilación de proteínas Alosterismo Histidin-quinasa Regulador de respuesta Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| dc.title.none.fl_str_mv | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| dc.type.none.fl_str_mv | Parte de libro info:eu-repo/semantics/bookPart Aceptado info:eu-repo/semantics/acceptedVersion |
| description | The ability to perceive the environment, an essential attribute in living organisms, is linked to the evolution of signalling proteins that recognize specific signals and execute predetermined responses. Such proteins constitute concerted systems that can be as simple as a unique protein, able to recognize a ligand and exert a phenotypic change, or extremely complex pathways engaging dozens of different proteins which act in coordination with feedback loops and signal modulation. To understand how cells sense their surroundings and mount specific adaptive responses, we need to decipher the molecular workings of signal recognition, internalization, transfer and conversion into chemical changes inside the cell. Protein allostery and dynamics play a central role. Here, we review recent progress on the study of two- component systems, important signalling machineries of prokaryotes and lower eukaryotes. Such systems implicate a sensory histidine-kinase and a separate response regulator protein. Both components exploit protein flexibility to effect specific conformational rearrangements, modulating protein:protein interactions, and ultimately transmitting information accurately. Recent work has revealed how histidine-kinases switch between discrete functional states according to the presence or absence of the signal, shifting key amino acid positions that define their catalytic activity. In concert with the cognate response regulator’s allosteric changes, the phosphoryl-transfer flow during the signalling process is exquisitely fine-tuned for proper specificity, efficiency and directionality. |
| eu_rights_str_mv | openAccess |
| format | bookPart |
| id | anni_3987f0f1b26a2ca36e33d1d89f1a74cd |
| identifier_str_mv | FCE_1_2017_1_136291 10.1007/978-1-4939-9884-5_1 |
| instacron_str | Institut Pasteur de Montevideo |
| institution | Institut Pasteur de Montevideo |
| instname_str | Institut Pasteur de Montevideo |
| language | eng |
| network_acronym_str | anni |
| network_name_str | oai-lr-anni |
| oai_identifier_str | oai:redi.anii.org.uy:20.500.12381/602 |
| publishDate | 2020 |
| publishDateSort | 2020 |
| publisher.none.fl_str_mv | Springer Nature (Humana Press) |
| reponame_str | IPMON en REDI |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | Acceso abierto Reconocimiento-NoComercial-SinObraDerivada 4.0 Internacional. (CC BY-NC-ND) |
| spelling | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component SystemsTrajtenberg, FelipeBuschiazzo, Alejandroseñalización bacterianaFosforilación de proteínasAlosterismoHistidin-quinasaRegulador de respuestaCiencias Naturales y ExactasCiencias BiológicasBioquímica y Biología MolecularThe ability to perceive the environment, an essential attribute in living organisms, is linked to the evolution of signalling proteins that recognize specific signals and execute predetermined responses. Such proteins constitute concerted systems that can be as simple as a unique protein, able to recognize a ligand and exert a phenotypic change, or extremely complex pathways engaging dozens of different proteins which act in coordination with feedback loops and signal modulation. To understand how cells sense their surroundings and mount specific adaptive responses, we need to decipher the molecular workings of signal recognition, internalization, transfer and conversion into chemical changes inside the cell. Protein allostery and dynamics play a central role. Here, we review recent progress on the study of two- component systems, important signalling machineries of prokaryotes and lower eukaryotes. Such systems implicate a sensory histidine-kinase and a separate response regulator protein. Both components exploit protein flexibility to effect specific conformational rearrangements, modulating protein:protein interactions, and ultimately transmitting information accurately. Recent work has revealed how histidine-kinases switch between discrete functional states according to the presence or absence of the signal, shifting key amino acid positions that define their catalytic activity. In concert with the cognate response regulator’s allosteric changes, the phosphoryl-transfer flow during the signalling process is exquisitely fine-tuned for proper specificity, efficiency and directionality.Agencia Nacional de Investigación e InnovaciónSpringer Nature (Humana Press)2022-07-01T14:02:33Z2022-07-01T14:02:33Z2020Parte de libroinfo:eu-repo/semantics/bookPartAceptadoinfo:eu-repo/semantics/acceptedVersionhttps://hdl.handle.net/20.500.12381/602FCE_1_2017_1_13629110.1007/978-1-4939-9884-5_1Histidine Phosphorylation - Methods and Protocolsreponame:IPMON en REDIinstname:Institut Pasteur de Montevideoinstacron:Institut Pasteur de Montevideoenghttps://hdl.handle.net/20.500.12381/603https://hdl.handle.net/20.500.12381/604Acceso abiertoinfo:eu-repo/semantics/openAccessReconocimiento-NoComercial-SinObraDerivada 4.0 Internacional. (CC BY-NC-ND)oai:redi.anii.org.uy:20.500.12381/6022026-06-16T05:20:27Z |
| spellingShingle | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems Trajtenberg, Felipe señalización bacteriana Fosforilación de proteínas Alosterismo Histidin-quinasa Regulador de respuesta Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| status_str | acceptedVersion |
| title | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| title_full | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| title_fullStr | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| title_full_unstemmed | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| title_short | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| title_sort | Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems |
| topic | señalización bacteriana Fosforilación de proteínas Alosterismo Histidin-quinasa Regulador de respuesta Ciencias Naturales y Exactas Ciencias Biológicas Bioquímica y Biología Molecular |
| url | https://hdl.handle.net/20.500.12381/602 |