Author(s): Taboada, Carlos ; Brunetti, Andres E. ; Lyra, Mariana L. [UNESP] ; Fitak, Robert R. ; Faigon Soverna, Ana ; Ron, Santiago R. ; Lagorio, Maria G. ; Haddad, Celio F. B. [UNESP] ; Lopes, Norberto P. ; Johnsen, Sonke ; Faivovich, Julian ; Chemes, Lucia B. ; Bari, Sara E.
Date: 2021
Persistent ID: http://hdl.handle.net/11449/209508
Origin: Oasisbr
Made available in DSpace on 2021-06-25T12:20:40Z (GMT). No. of bitstreams: 0 Previous issue date: 2020-08-04
Human Frontier Science Program
Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Agencia Nacional de Promocion Cientifica y Tecnologica, Proyecto de Investigacion Cientifica y Tecnologica
CONICET
Universidad de Buenos Aires
Universidad de Buenos Aires Ciencia y Tecnica
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Secretaria Nacional de Educacion Superior, Ciencia, Tecnologia e Innovacion del Ecuador (SENESCYT) (Arca de Noe initiative)
Direccion General Academica Pontificia Universidad Catolica del Ecuador
Many vertebrates have distinctive blue-green bones and other tissues due to unusually high biliverdin concentrations-a phenomenon called chlorosis. Despite its prevalence, the biochemical basis, biology, and evolution of chlorosis are poorly understood. In this study, we show that the occurrence of high biliverdin in anurans (frogs and toads) has evolved multiple times during their evolutionary history, and relies on the same mechanism-the presence of a class of serpin family proteins that bind biliverdin. Using a diverse combination of techniques, we purified these serpins from several species of nonmodel treefrogs and developed a pipeline that allowed us to assemble their complete amino acid and nucleotide sequences. The described proteins, hereafter named biliverdin-binding serpins (BBS), have absorption spectra that mimic those of phytochromes and bacteriophytochromes. Our models showed that physiological concentration of BBS5 fine-tune the color of the animals, providing the physiological basis for crypsis in green foliage even under near-infrared light. Additionally, we found that these BBS5 are most similar to human glycoprotein alpha-1-antitrypsin, but with a remarkable functional diversification. Our results present molecular and functional evidence of recurrent evolution of chlorosis, describe a biliverdin-binding protein in vertebrates, and introduce a function for a member of the serpin superfamily, the largest and most ubiquitous group of protease inhibitors.
Duke Univ, Dept Biol, Durham, NC 27708 USA
Consejo Nacl Invest Cient & Tecn CONICET, Museo Argentino Ciencias Nat Bernardino Rivadavia, Div Herpetol, C1405DJR, Buenos Aires, DF, Argentina
Univ Buenos Aires, Fac Ciencias Exactas & Nat, Inst Quim Fis Mat Medio Ambiente & Energia, Consejo Nacl Invest Cient & Tecn CONICET, C1428EHA, Buenos Aires, DF, Argentina
Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Ciencias BioMol, Nucleo Pesquisa Prod Nat & Sintet NPPNS, BR-14040903 Ribeirao Preto, SP, Brazil
Univ Nacl Misiones, Fac Ciencias Exactas, Inst Biol Subtrop CONICET UNaM, Lab Genet Evolut Claudio Juan Bidau, RA-3300 Posadas, Misiones, Argentina
Univ Estadual Paulista, Dept Biodiversidade, BR-13506900 Rio Claro, SP, Brazil
Univ Estadual Paulista, Ctr Aquicultura, Inst Biociencias, BR-13506900 Rio Claro, SP, Brazil
Univ Cent Florida, Dept Biol Genom & Bioinformat Cluster, Orlando, FL 32816 USA
Pontificia Univ CatOlica Ecuador, Escuela Biol, Museo Zool, Aptdo 17-01-2184, Quito, Ecuador
Univ Buenos Aires, Fac Ciencias Exactas & Nat, Dept Quim Inorgan Analit & Quim Fis, C1428EHA, Buenos Aires, DF, Argentina
Univ Buenos Aires, Fac Ciencias Exactas & Nat, Dept Biodiversidad & Biol Expt, C1428EHA, Buenos Aires, DF, Argentina
Consejo Nacl Invest Cient & Tecn, Fdn Inst Leloir, C1405BWE, Buenos Aires, DF, Argentina
Consejo Nacl Invest Cient & Tecn, Inst Invest Bioquim Buenos Aires, C1405BWE, Buenos Aires, DF, Argentina
Univ Nacl San Martin, Inst Invest Biotecnol, RA-1650 San Martin, Buenos Aires, Argentina
Univ Estadual Paulista, Dept Biodiversidade, BR-13506900 Rio Claro, SP, Brazil
Univ Estadual Paulista, Ctr Aquicultura, Inst Biociencias, BR-13506900 Rio Claro, SP, Brazil
Human Frontier Science Program: LT 000660/2018-L
FAPESP: 2014/20915-6
FAPESP: 2017/23725-1
FAPESP: 2017/26162-8
Agencia Nacional de Promocion Cientifica y Tecnologica, Proyecto de Investigacion Cientifica y Tecnologica: 2011-1895
Agencia Nacional de Promocion Cientifica y Tecnologica, Proyecto de Investigacion Cientifica y Tecnologica: 2013-404
Agencia Nacional de Promocion Cientifica y Tecnologica, Proyecto de Investigacion Cientifica y Tecnologica: 2013-1895
Agencia Nacional de Promocion Cientifica y Tecnologica, Proyecto de Investigacion Cientifica y Tecnologica: 2014-1022
Agencia Nacional de Promocion Cientifica y Tecnologica, Proyecto de Investigacion Cientifica y Tecnologica: 2015-820
CONICET: 11220150100394CO
Universidad de Buenos Aires Ciencia y Tecnica: 20020170100037BA
FAPESP: 2013/50741-7
FAPESP: 2012/10000-5
FAPESP: 2014/50342-8
FAPESP: 2018/15425-0
CNPq: 306623/2018-8
