Drosophila melanogaster mutant tan

Autores
Badaracco, Alejandra; Quesada Allue, Luis Alberto; Pérez, Martín Mariano
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Drosophila melanogaster gene tan was originally discovered in the early 20th century as a mutant strain lacking the dark pi gment pattern of wild-type (wt) f lies and, therefore, showing a light yellowish brown color (McEwen, 1918). Flies lack ing Tan function also exhibited abnormalities in vision (Benzer, 1967; Inoue et al. , 1988; True et al. , 2005), and tan males displayed an abnormal courtship behavior (Cook, 1980; Tomkins et al. , 1982). tan 1 ( t 1 ) and tan 3 ( t 3 ) alleles were found as spontaneous mutations, t 3 mutant being apparently lighter than t 1 (Brehme, 1941). tan is the structural gene for N- β -alanyldopamine hydrolase (NBAD-hydrolase or Tan protein), the enzyme that generates dopamine (DA) from NBAD (Wright, 1987; True et al. , 2005). Tan is expressed as a precursor protein of 43.7 kDa. Th is precursor is clea ved into two subunits of 29.9 and 13.8 kDa that apparently conform together a he terodimeric active protein (Wagner et al. , 2007). The enzyme that generates NBAD from DA, th e opposite reaction to the one catalyzed by Tan, is the NBAD-synthase or E bony protein (Wright, 1987; Pérez et al ., 1997), which is codified by the gene ebony . Since both Tan and Ebony ar e involved in cuticle tanni ng, carcinine re gulation, and NBAD metabolism in nervous tissue (Wright, 1987; Pérez et al. , 1997, 2004; Hovemann et al. , 1998; Borycz et al. , 2002; True et al. , 2005), it has been suggested that they function together in a system regulating the levels of dopamine during cuticle sclerotization a nd histamine in the visual metabolism (Borycz et al. , 2002; Pérez et al. , 2010). During the last few years, several publicati ons appeared regarding NBAD-synthase (Wappner et al ., 1996a, b; Pérez et al ., 1997, 2002, 2004, 2010; Hovemann et al. , 1998; Borycz et al. , 2002; Wittkopp et al., 2002; Schachter et al ., 2007), but very little is known about tan (True et al. , 2005; Wagner et al. , 2007). Thus, it was important to furthe r characterize the NBAD-hydrolase in D. melanogaster wt and in mutants t 1 and t 3.
Fil: Badaracco, Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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: Quesada Allue, Luis Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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: Pérez, Martín Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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
Materia
HYDROLASE
NERVOUS SYSTEM
SCLEROTIZATION
BETA-ALANILDERIVATIVES
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:11336/38872

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spelling Drosophila melanogaster mutant tanBadaracco, AlejandraQuesada Allue, Luis AlbertoPérez, Martín MarianoHYDROLASENERVOUS SYSTEMSCLEROTIZATIONBETA-ALANILDERIVATIVEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Drosophila melanogaster gene tan was originally discovered in the early 20th century as a mutant strain lacking the dark pi gment pattern of wild-type (wt) f lies and, therefore, showing a light yellowish brown color (McEwen, 1918). Flies lack ing Tan function also exhibited abnormalities in vision (Benzer, 1967; Inoue et al. , 1988; True et al. , 2005), and tan males displayed an abnormal courtship behavior (Cook, 1980; Tomkins et al. , 1982). tan 1 ( t 1 ) and tan 3 ( t 3 ) alleles were found as spontaneous mutations, t 3 mutant being apparently lighter than t 1 (Brehme, 1941). tan is the structural gene for N- β -alanyldopamine hydrolase (NBAD-hydrolase or Tan protein), the enzyme that generates dopamine (DA) from NBAD (Wright, 1987; True et al. , 2005). Tan is expressed as a precursor protein of 43.7 kDa. Th is precursor is clea ved into two subunits of 29.9 and 13.8 kDa that apparently conform together a he terodimeric active protein (Wagner et al. , 2007). The enzyme that generates NBAD from DA, th e opposite reaction to the one catalyzed by Tan, is the NBAD-synthase or E bony protein (Wright, 1987; Pérez et al ., 1997), which is codified by the gene ebony . Since both Tan and Ebony ar e involved in cuticle tanni ng, carcinine re gulation, and NBAD metabolism in nervous tissue (Wright, 1987; Pérez et al. , 1997, 2004; Hovemann et al. , 1998; Borycz et al. , 2002; True et al. , 2005), it has been suggested that they function together in a system regulating the levels of dopamine during cuticle sclerotization a nd histamine in the visual metabolism (Borycz et al. , 2002; Pérez et al. , 2010). During the last few years, several publicati ons appeared regarding NBAD-synthase (Wappner et al ., 1996a, b; Pérez et al ., 1997, 2002, 2004, 2010; Hovemann et al. , 1998; Borycz et al. , 2002; Wittkopp et al., 2002; Schachter et al ., 2007), but very little is known about tan (True et al. , 2005; Wagner et al. , 2007). Thus, it was important to furthe r characterize the NBAD-hydrolase in D. melanogaster wt and in mutants t 1 and t 3.Fil: Badaracco, Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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: Quesada Allue, Luis Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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: Pérez, Martín Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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; ArgentinaUniversity of Oklahoma2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/38872Badaracco, Alejandra; Quesada Allue, Luis Alberto; Pérez, Martín Mariano; Drosophila melanogaster mutant tan; University of Oklahoma; Drosophila Information Service; 92; 12-2009; 90-930070-7333CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.ou.edu/journals/dis/DIS92/Badaracco%2090.pdfinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:52:06Zoai:ri.conicet.gov.ar:11336/38872instacron: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 09:52:07.147CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Drosophila melanogaster mutant tan
title Drosophila melanogaster mutant tan
spellingShingle Drosophila melanogaster mutant tan
Badaracco, Alejandra
HYDROLASE
NERVOUS SYSTEM
SCLEROTIZATION
BETA-ALANILDERIVATIVES
title_short Drosophila melanogaster mutant tan
title_full Drosophila melanogaster mutant tan
title_fullStr Drosophila melanogaster mutant tan
title_full_unstemmed Drosophila melanogaster mutant tan
title_sort Drosophila melanogaster mutant tan
dc.creator.none.fl_str_mv Badaracco, Alejandra
Quesada Allue, Luis Alberto
Pérez, Martín Mariano
author Badaracco, Alejandra
author_facet Badaracco, Alejandra
Quesada Allue, Luis Alberto
Pérez, Martín Mariano
author_role author
author2 Quesada Allue, Luis Alberto
Pérez, Martín Mariano
author2_role author
author
dc.subject.none.fl_str_mv HYDROLASE
NERVOUS SYSTEM
SCLEROTIZATION
BETA-ALANILDERIVATIVES
topic HYDROLASE
NERVOUS SYSTEM
SCLEROTIZATION
BETA-ALANILDERIVATIVES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Drosophila melanogaster gene tan was originally discovered in the early 20th century as a mutant strain lacking the dark pi gment pattern of wild-type (wt) f lies and, therefore, showing a light yellowish brown color (McEwen, 1918). Flies lack ing Tan function also exhibited abnormalities in vision (Benzer, 1967; Inoue et al. , 1988; True et al. , 2005), and tan males displayed an abnormal courtship behavior (Cook, 1980; Tomkins et al. , 1982). tan 1 ( t 1 ) and tan 3 ( t 3 ) alleles were found as spontaneous mutations, t 3 mutant being apparently lighter than t 1 (Brehme, 1941). tan is the structural gene for N- β -alanyldopamine hydrolase (NBAD-hydrolase or Tan protein), the enzyme that generates dopamine (DA) from NBAD (Wright, 1987; True et al. , 2005). Tan is expressed as a precursor protein of 43.7 kDa. Th is precursor is clea ved into two subunits of 29.9 and 13.8 kDa that apparently conform together a he terodimeric active protein (Wagner et al. , 2007). The enzyme that generates NBAD from DA, th e opposite reaction to the one catalyzed by Tan, is the NBAD-synthase or E bony protein (Wright, 1987; Pérez et al ., 1997), which is codified by the gene ebony . Since both Tan and Ebony ar e involved in cuticle tanni ng, carcinine re gulation, and NBAD metabolism in nervous tissue (Wright, 1987; Pérez et al. , 1997, 2004; Hovemann et al. , 1998; Borycz et al. , 2002; True et al. , 2005), it has been suggested that they function together in a system regulating the levels of dopamine during cuticle sclerotization a nd histamine in the visual metabolism (Borycz et al. , 2002; Pérez et al. , 2010). During the last few years, several publicati ons appeared regarding NBAD-synthase (Wappner et al ., 1996a, b; Pérez et al ., 1997, 2002, 2004, 2010; Hovemann et al. , 1998; Borycz et al. , 2002; Wittkopp et al., 2002; Schachter et al ., 2007), but very little is known about tan (True et al. , 2005; Wagner et al. , 2007). Thus, it was important to furthe r characterize the NBAD-hydrolase in D. melanogaster wt and in mutants t 1 and t 3.
Fil: Badaracco, Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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: Quesada Allue, Luis Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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: Pérez, Martín Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. 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
description Drosophila melanogaster gene tan was originally discovered in the early 20th century as a mutant strain lacking the dark pi gment pattern of wild-type (wt) f lies and, therefore, showing a light yellowish brown color (McEwen, 1918). Flies lack ing Tan function also exhibited abnormalities in vision (Benzer, 1967; Inoue et al. , 1988; True et al. , 2005), and tan males displayed an abnormal courtship behavior (Cook, 1980; Tomkins et al. , 1982). tan 1 ( t 1 ) and tan 3 ( t 3 ) alleles were found as spontaneous mutations, t 3 mutant being apparently lighter than t 1 (Brehme, 1941). tan is the structural gene for N- β -alanyldopamine hydrolase (NBAD-hydrolase or Tan protein), the enzyme that generates dopamine (DA) from NBAD (Wright, 1987; True et al. , 2005). Tan is expressed as a precursor protein of 43.7 kDa. Th is precursor is clea ved into two subunits of 29.9 and 13.8 kDa that apparently conform together a he terodimeric active protein (Wagner et al. , 2007). The enzyme that generates NBAD from DA, th e opposite reaction to the one catalyzed by Tan, is the NBAD-synthase or E bony protein (Wright, 1987; Pérez et al ., 1997), which is codified by the gene ebony . Since both Tan and Ebony ar e involved in cuticle tanni ng, carcinine re gulation, and NBAD metabolism in nervous tissue (Wright, 1987; Pérez et al. , 1997, 2004; Hovemann et al. , 1998; Borycz et al. , 2002; True et al. , 2005), it has been suggested that they function together in a system regulating the levels of dopamine during cuticle sclerotization a nd histamine in the visual metabolism (Borycz et al. , 2002; Pérez et al. , 2010). During the last few years, several publicati ons appeared regarding NBAD-synthase (Wappner et al ., 1996a, b; Pérez et al ., 1997, 2002, 2004, 2010; Hovemann et al. , 1998; Borycz et al. , 2002; Wittkopp et al., 2002; Schachter et al ., 2007), but very little is known about tan (True et al. , 2005; Wagner et al. , 2007). Thus, it was important to furthe r characterize the NBAD-hydrolase in D. melanogaster wt and in mutants t 1 and t 3.
publishDate 2009
dc.date.none.fl_str_mv 2009-12
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/11336/38872
Badaracco, Alejandra; Quesada Allue, Luis Alberto; Pérez, Martín Mariano; Drosophila melanogaster mutant tan; University of Oklahoma; Drosophila Information Service; 92; 12-2009; 90-93
0070-7333
CONICET Digital
CONICET
url http://hdl.handle.net/11336/38872
identifier_str_mv Badaracco, Alejandra; Quesada Allue, Luis Alberto; Pérez, Martín Mariano; Drosophila melanogaster mutant tan; University of Oklahoma; Drosophila Information Service; 92; 12-2009; 90-93
0070-7333
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.ou.edu/journals/dis/DIS92/Badaracco%2090.pdf
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv University of Oklahoma
publisher.none.fl_str_mv University of Oklahoma
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
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