Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2

Autores
Fago, Angela; Natarajan, Chandrasekhar; Pettinati, Martín; Hoffmann, Federico G.; Wang, Tobias; Weber, Roy E.; Drusin, Salvador Iván; Issoglio, Federico Matías; Marti, Marcelo Adrian; Estrin, Dario Ariel; Storz, Jay F.
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Hemoglobins (Hbs) of crocodilians are reportedly characterized by unique mechanisms of allosteric regulatory control, but there are conflicting reports regarding the importance of different effectors, such as chloride ions, organic phosphates, and CO2. Progress in understanding the unusual properties of crocodilian Hbs has also been hindered by a dearth of structural information. Here, we present the first comparative analysis of blood properties and Hb structure and function in a phylogenetically diverse set of crocodilian species. We examine mechanisms of allosteric regulation in the Hbs of 13 crocodilian species belonging to the families Crocodylidae and Alligatoridae. We also report new amino acid sequences for the α- and β-globins of these taxa, which, in combination with structural analyses, provide insights into molecular mechanisms of allosteric regulation. All crocodilian Hbs exhibited a remarkably strong sensitivity to CO2, which would permit effective O2 unloading to tissues in response to an increase in metabolism during intense activity and diving. Although the Hbs of all crocodilians exhibit similar intrinsic O2-affinities, there is considerable variation in sensitivity to Cl- ions and ATP, which appears to be at least partly attributable to variation in the extent of NH2-terminal acetylation. Whereas chloride appears to be a potent allosteric effector of all crocodile Hbs, ATP has a strong, chloride-independent effect on Hb-O2 affinity only in caimans. Modeling suggests that allosteric ATP binding has a somewhat different structural basis in crocodilian and mammalian Hbs.
Fil: Fago, Angela. University Aarhus; Dinamarca
Fil: Natarajan, Chandrasekhar. University of Nebraska; Estados Unidos
Fil: Pettinati, Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Hoffmann, Federico G.. Mississippi State University; Estados Unidos
Fil: Wang, Tobias. University Aarhus; Dinamarca
Fil: Weber, Roy E.. University Aarhus; Dinamarca
Fil: Drusin, Salvador Iván. 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
Fil: Issoglio, Federico Matías. 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
Fil: Marti, Marcelo Adrian. 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
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Storz, Jay F.. University of Nebraska; Estados Unidos
Materia
ADAPTATION
ALLOSTERY
BLOOD
OXYGEN TRANSPORT
REPTILE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/143924
Acceder
id CONICETDig_6bb07ba4c7d03c7c2482ec09b63b899e
oai_identifier_str oai:ri.conicet.gov.ar:11336/143924
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2Fago, AngelaNatarajan, ChandrasekharPettinati, MartínHoffmann, Federico G.Wang, TobiasWeber, Roy E.Drusin, Salvador IvánIssoglio, Federico MatíasMarti, Marcelo AdrianEstrin, Dario ArielStorz, Jay F.ADAPTATIONALLOSTERYBLOODOXYGEN TRANSPORTREPTILEhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Hemoglobins (Hbs) of crocodilians are reportedly characterized by unique mechanisms of allosteric regulatory control, but there are conflicting reports regarding the importance of different effectors, such as chloride ions, organic phosphates, and CO2. Progress in understanding the unusual properties of crocodilian Hbs has also been hindered by a dearth of structural information. Here, we present the first comparative analysis of blood properties and Hb structure and function in a phylogenetically diverse set of crocodilian species. We examine mechanisms of allosteric regulation in the Hbs of 13 crocodilian species belonging to the families Crocodylidae and Alligatoridae. We also report new amino acid sequences for the α- and β-globins of these taxa, which, in combination with structural analyses, provide insights into molecular mechanisms of allosteric regulation. All crocodilian Hbs exhibited a remarkably strong sensitivity to CO2, which would permit effective O2 unloading to tissues in response to an increase in metabolism during intense activity and diving. Although the Hbs of all crocodilians exhibit similar intrinsic O2-affinities, there is considerable variation in sensitivity to Cl- ions and ATP, which appears to be at least partly attributable to variation in the extent of NH2-terminal acetylation. Whereas chloride appears to be a potent allosteric effector of all crocodile Hbs, ATP has a strong, chloride-independent effect on Hb-O2 affinity only in caimans. Modeling suggests that allosteric ATP binding has a somewhat different structural basis in crocodilian and mammalian Hbs.Fil: Fago, Angela. University Aarhus; DinamarcaFil: Natarajan, Chandrasekhar. University of Nebraska; Estados UnidosFil: Pettinati, Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Hoffmann, Federico G.. Mississippi State University; Estados UnidosFil: Wang, Tobias. University Aarhus; DinamarcaFil: Weber, Roy E.. University Aarhus; DinamarcaFil: Drusin, Salvador Iván. 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; ArgentinaFil: Issoglio, Federico Matías. 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; ArgentinaFil: Marti, Marcelo Adrian. 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; ArgentinaFil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Storz, Jay F.. University of Nebraska; Estados UnidosAmerican Physiological Society2020-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/143924Fago, Angela; Natarajan, Chandrasekhar; Pettinati, Martín; Hoffmann, Federico G.; Wang, Tobias; et al.; Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2; American Physiological Society; American Journal of Physiology: Regulatory, Integrative and Comparative Physiology; 318; 3; 3-2020; R657-R6670363-6119CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.physiology.org/doi/10.1152/ajpregu.00342.2019info:eu-repo/semantics/altIdentifier/doi/10.1152/ajpregu.00342.2019info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:31Zoai:ri.conicet.gov.ar:11336/143924instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:04:32.165CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
title Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
spellingShingle Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
Fago, Angela
ADAPTATION
ALLOSTERY
BLOOD
OXYGEN TRANSPORT
REPTILE
title_short Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
title_full Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
title_fullStr Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
title_full_unstemmed Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
title_sort Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2
dc.creator.none.fl_str_mv Fago, Angela
Natarajan, Chandrasekhar
Pettinati, Martín
Hoffmann, Federico G.
Wang, Tobias
Weber, Roy E.
Drusin, Salvador Iván
Issoglio, Federico Matías
Marti, Marcelo Adrian
Estrin, Dario Ariel
Storz, Jay F.
author Fago, Angela
author_facet Fago, Angela
Natarajan, Chandrasekhar
Pettinati, Martín
Hoffmann, Federico G.
Wang, Tobias
Weber, Roy E.
Drusin, Salvador Iván
Issoglio, Federico Matías
Marti, Marcelo Adrian
Estrin, Dario Ariel
Storz, Jay F.
author_role author
author2 Natarajan, Chandrasekhar
Pettinati, Martín
Hoffmann, Federico G.
Wang, Tobias
Weber, Roy E.
Drusin, Salvador Iván
Issoglio, Federico Matías
Marti, Marcelo Adrian
Estrin, Dario Ariel
Storz, Jay F.
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ADAPTATION
ALLOSTERY
BLOOD
OXYGEN TRANSPORT
REPTILE
topic ADAPTATION
ALLOSTERY
BLOOD
OXYGEN TRANSPORT
REPTILE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Hemoglobins (Hbs) of crocodilians are reportedly characterized by unique mechanisms of allosteric regulatory control, but there are conflicting reports regarding the importance of different effectors, such as chloride ions, organic phosphates, and CO2. Progress in understanding the unusual properties of crocodilian Hbs has also been hindered by a dearth of structural information. Here, we present the first comparative analysis of blood properties and Hb structure and function in a phylogenetically diverse set of crocodilian species. We examine mechanisms of allosteric regulation in the Hbs of 13 crocodilian species belonging to the families Crocodylidae and Alligatoridae. We also report new amino acid sequences for the α- and β-globins of these taxa, which, in combination with structural analyses, provide insights into molecular mechanisms of allosteric regulation. All crocodilian Hbs exhibited a remarkably strong sensitivity to CO2, which would permit effective O2 unloading to tissues in response to an increase in metabolism during intense activity and diving. Although the Hbs of all crocodilians exhibit similar intrinsic O2-affinities, there is considerable variation in sensitivity to Cl- ions and ATP, which appears to be at least partly attributable to variation in the extent of NH2-terminal acetylation. Whereas chloride appears to be a potent allosteric effector of all crocodile Hbs, ATP has a strong, chloride-independent effect on Hb-O2 affinity only in caimans. Modeling suggests that allosteric ATP binding has a somewhat different structural basis in crocodilian and mammalian Hbs.
Fil: Fago, Angela. University Aarhus; Dinamarca
Fil: Natarajan, Chandrasekhar. University of Nebraska; Estados Unidos
Fil: Pettinati, Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Hoffmann, Federico G.. Mississippi State University; Estados Unidos
Fil: Wang, Tobias. University Aarhus; Dinamarca
Fil: Weber, Roy E.. University Aarhus; Dinamarca
Fil: Drusin, Salvador Iván. 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
Fil: Issoglio, Federico Matías. 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
Fil: Marti, Marcelo Adrian. 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
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Storz, Jay F.. University of Nebraska; Estados Unidos
description Hemoglobins (Hbs) of crocodilians are reportedly characterized by unique mechanisms of allosteric regulatory control, but there are conflicting reports regarding the importance of different effectors, such as chloride ions, organic phosphates, and CO2. Progress in understanding the unusual properties of crocodilian Hbs has also been hindered by a dearth of structural information. Here, we present the first comparative analysis of blood properties and Hb structure and function in a phylogenetically diverse set of crocodilian species. We examine mechanisms of allosteric regulation in the Hbs of 13 crocodilian species belonging to the families Crocodylidae and Alligatoridae. We also report new amino acid sequences for the α- and β-globins of these taxa, which, in combination with structural analyses, provide insights into molecular mechanisms of allosteric regulation. All crocodilian Hbs exhibited a remarkably strong sensitivity to CO2, which would permit effective O2 unloading to tissues in response to an increase in metabolism during intense activity and diving. Although the Hbs of all crocodilians exhibit similar intrinsic O2-affinities, there is considerable variation in sensitivity to Cl- ions and ATP, which appears to be at least partly attributable to variation in the extent of NH2-terminal acetylation. Whereas chloride appears to be a potent allosteric effector of all crocodile Hbs, ATP has a strong, chloride-independent effect on Hb-O2 affinity only in caimans. Modeling suggests that allosteric ATP binding has a somewhat different structural basis in crocodilian and mammalian Hbs.
publishDate 2020
dc.date.none.fl_str_mv 2020-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/143924
Fago, Angela; Natarajan, Chandrasekhar; Pettinati, Martín; Hoffmann, Federico G.; Wang, Tobias; et al.; Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2; American Physiological Society; American Journal of Physiology: Regulatory, Integrative and Comparative Physiology; 318; 3; 3-2020; R657-R667
0363-6119
CONICET Digital
CONICET
url http://hdl.handle.net/11336/143924
identifier_str_mv Fago, Angela; Natarajan, Chandrasekhar; Pettinati, Martín; Hoffmann, Federico G.; Wang, Tobias; et al.; Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2; American Physiological Society; American Journal of Physiology: Regulatory, Integrative and Comparative Physiology; 318; 3; 3-2020; R657-R667
0363-6119
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.physiology.org/doi/10.1152/ajpregu.00342.2019
info:eu-repo/semantics/altIdentifier/doi/10.1152/ajpregu.00342.2019
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Physiological Society
publisher.none.fl_str_mv American Physiological Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269860881498112
score 13.13397

Publicaciones similares