Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate

Detalhes bibliográficos
Autor(a) principal: Suzuki, J. [UNESP]
Data de Publicação: 2003
Outros Autores: Mutton, M. A. [UNESP], Ferro, M. I T [UNESP], Lemos, M. V F [UNESP], Pizauro, J. M. [UNESP], Mutton, M. J R [UNESP], Di Mauro, S. M Z [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://www.geneticsmr.com//year2003/vol2-4/pdf/gmr0065.pdf
http://hdl.handle.net/11449/67545
Resumo: Pyrophosphate-dependent phosphofructokinase (PPi-PFK) has been detected in several types of plant cells, but the gene has not been reported in sugar cane. Using Citrux paradixi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have identified both the α and β subunits of this enzyme. The deduced amino acid sequences showed 76 and 80% similarity with the corresponding α and β subunits of C. paradisi. A high degree of similarity was also observed among the PFK β subunits when the alignment of the sugar cane sequences was compared to those of Ricinus communis and Solanum tuberosum, it appears that α and β are two distinct subunits; they were found at different concentrations in several sugar cane tissues. It remains to be determined if the different gene expression levels have some physiological importance and how they affect sucrose synthesis, export, and storage in vacuoles. A comparison between the amino acid sequences of β PFKs from a variety of organisms allowed us to identify the two critical Asp residues typical of this enzyme's activity site and the other binding sites; these residues are tightly conserved in all members of this protein family. Apparently, there are catalytic residues on the β subunit of the pyrophosphate-dependent enzyme.
id UNSP_1ba1dd89035842adbcf6628bd77d6c41
oai_identifier_str oai:repositorio.unesp.br:11449/67545
network_acronym_str UNSP
network_name_str Repositório Institucional da UNESP
repository_id_str 2946
spelling Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphateATPPPi-PFKPyrophosphate phosphofructose 1-kinaseSucroseSucrose synthaseSugar canecomplementary DNAinorganic pyrophosphatasephosphotransferasepyrophosphate fructose 6 phosphate 1 phosphotransferasepyrophosphate-fructose 6-phosphate 1-phosphotransferasepyrophosphatepyrophosphate phosphofructose 1 kinasesucroseunclassified drugamino acid sequenceenzymologygeneticsmetabolismmolecular geneticssugarcanealpha chainbeta chaincarbohydrate synthesisDNA libraryenergy metabolismenzyme active siteenzyme bindingenzyme subunitexpressed sequence taggene expressiongene identificationgrapefruitnonhumanplant geneticsplant tissuepotatoRicinus communisspecies comparisontissue levelAmino Acid SequenceDNA, ComplementaryMolecular Sequence DataPhosphotransferasesPyrophosphatasesSaccharumArundinariaCitrus x paradisiSaccharum hybrid cultivarSolanumSolanum tuberosumPyrophosphate-dependent phosphofructokinase (PPi-PFK) has been detected in several types of plant cells, but the gene has not been reported in sugar cane. Using Citrux paradixi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have identified both the α and β subunits of this enzyme. The deduced amino acid sequences showed 76 and 80% similarity with the corresponding α and β subunits of C. paradisi. A high degree of similarity was also observed among the PFK β subunits when the alignment of the sugar cane sequences was compared to those of Ricinus communis and Solanum tuberosum, it appears that α and β are two distinct subunits; they were found at different concentrations in several sugar cane tissues. It remains to be determined if the different gene expression levels have some physiological importance and how they affect sucrose synthesis, export, and storage in vacuoles. A comparison between the amino acid sequences of β PFKs from a variety of organisms allowed us to identify the two critical Asp residues typical of this enzyme's activity site and the other binding sites; these residues are tightly conserved in all members of this protein family. Apparently, there are catalytic residues on the β subunit of the pyrophosphate-dependent enzyme.Departamento de Tecnologia Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPBrazilian Clone Collection Center Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPDepartamento de Producao Vegetal Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPDepto. de Biol. Apl. a Agropecuaria Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPDepartamento de Tecnologia Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPBrazilian Clone Collection Center Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPDepartamento de Producao Vegetal Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPDepto. de Biol. Apl. a Agropecuaria Fac. Cie. Agrarias/Vet. Jaboticabal UNESP, Jaboticabal, SPUniversidade Estadual Paulista (Unesp)Suzuki, J. [UNESP]Mutton, M. A. [UNESP]Ferro, M. I T [UNESP]Lemos, M. V F [UNESP]Pizauro, J. M. [UNESP]Mutton, M. J R [UNESP]Di Mauro, S. M Z [UNESP]2014-05-27T11:20:59Z2014-05-27T11:20:59Z2003-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article376-382application/pdfhttp://www.geneticsmr.com//year2003/vol2-4/pdf/gmr0065.pdfGenetics and Molecular Research, v. 2, n. 4, p. 376-382, 2003.1676-5680http://hdl.handle.net/11449/675452-s2.0-25424631072-s2.0-2542463107.pdf895114117257998571792730606247612663920223082171Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengGenetics and Molecular Research0,439info:eu-repo/semantics/openAccess2024-06-07T15:31:59Zoai:repositorio.unesp.br:11449/67545Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:06:19.485211Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
title Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
spellingShingle Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
Suzuki, J. [UNESP]
ATP
PPi-PFK
Pyrophosphate phosphofructose 1-kinase
Sucrose
Sucrose synthase
Sugar cane
complementary DNA
inorganic pyrophosphatase
phosphotransferase
pyrophosphate fructose 6 phosphate 1 phosphotransferase
pyrophosphate-fructose 6-phosphate 1-phosphotransferase
pyrophosphate
pyrophosphate phosphofructose 1 kinase
sucrose
unclassified drug
amino acid sequence
enzymology
genetics
metabolism
molecular genetics
sugarcane
alpha chain
beta chain
carbohydrate synthesis
DNA library
energy metabolism
enzyme active site
enzyme binding
enzyme subunit
expressed sequence tag
gene expression
gene identification
grapefruit
nonhuman
plant genetics
plant tissue
potato
Ricinus communis
species comparison
tissue level
Amino Acid Sequence
DNA, Complementary
Molecular Sequence Data
Phosphotransferases
Pyrophosphatases
Saccharum
Arundinaria
Citrus x paradisi
Saccharum hybrid cultivar
Solanum
Solanum tuberosum
title_short Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
title_full Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
title_fullStr Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
title_full_unstemmed Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
title_sort Putative pyrophosphate phosphofructose 1-kinase genes identified in sugarcane may be getting energy from pyrophosphate
author Suzuki, J. [UNESP]
author_facet Suzuki, J. [UNESP]
Mutton, M. A. [UNESP]
Ferro, M. I T [UNESP]
Lemos, M. V F [UNESP]
Pizauro, J. M. [UNESP]
Mutton, M. J R [UNESP]
Di Mauro, S. M Z [UNESP]
author_role author
author2 Mutton, M. A. [UNESP]
Ferro, M. I T [UNESP]
Lemos, M. V F [UNESP]
Pizauro, J. M. [UNESP]
Mutton, M. J R [UNESP]
Di Mauro, S. M Z [UNESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Suzuki, J. [UNESP]
Mutton, M. A. [UNESP]
Ferro, M. I T [UNESP]
Lemos, M. V F [UNESP]
Pizauro, J. M. [UNESP]
Mutton, M. J R [UNESP]
Di Mauro, S. M Z [UNESP]
dc.subject.por.fl_str_mv ATP
PPi-PFK
Pyrophosphate phosphofructose 1-kinase
Sucrose
Sucrose synthase
Sugar cane
complementary DNA
inorganic pyrophosphatase
phosphotransferase
pyrophosphate fructose 6 phosphate 1 phosphotransferase
pyrophosphate-fructose 6-phosphate 1-phosphotransferase
pyrophosphate
pyrophosphate phosphofructose 1 kinase
sucrose
unclassified drug
amino acid sequence
enzymology
genetics
metabolism
molecular genetics
sugarcane
alpha chain
beta chain
carbohydrate synthesis
DNA library
energy metabolism
enzyme active site
enzyme binding
enzyme subunit
expressed sequence tag
gene expression
gene identification
grapefruit
nonhuman
plant genetics
plant tissue
potato
Ricinus communis
species comparison
tissue level
Amino Acid Sequence
DNA, Complementary
Molecular Sequence Data
Phosphotransferases
Pyrophosphatases
Saccharum
Arundinaria
Citrus x paradisi
Saccharum hybrid cultivar
Solanum
Solanum tuberosum
topic ATP
PPi-PFK
Pyrophosphate phosphofructose 1-kinase
Sucrose
Sucrose synthase
Sugar cane
complementary DNA
inorganic pyrophosphatase
phosphotransferase
pyrophosphate fructose 6 phosphate 1 phosphotransferase
pyrophosphate-fructose 6-phosphate 1-phosphotransferase
pyrophosphate
pyrophosphate phosphofructose 1 kinase
sucrose
unclassified drug
amino acid sequence
enzymology
genetics
metabolism
molecular genetics
sugarcane
alpha chain
beta chain
carbohydrate synthesis
DNA library
energy metabolism
enzyme active site
enzyme binding
enzyme subunit
expressed sequence tag
gene expression
gene identification
grapefruit
nonhuman
plant genetics
plant tissue
potato
Ricinus communis
species comparison
tissue level
Amino Acid Sequence
DNA, Complementary
Molecular Sequence Data
Phosphotransferases
Pyrophosphatases
Saccharum
Arundinaria
Citrus x paradisi
Saccharum hybrid cultivar
Solanum
Solanum tuberosum
description Pyrophosphate-dependent phosphofructokinase (PPi-PFK) has been detected in several types of plant cells, but the gene has not been reported in sugar cane. Using Citrux paradixi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have identified both the α and β subunits of this enzyme. The deduced amino acid sequences showed 76 and 80% similarity with the corresponding α and β subunits of C. paradisi. A high degree of similarity was also observed among the PFK β subunits when the alignment of the sugar cane sequences was compared to those of Ricinus communis and Solanum tuberosum, it appears that α and β are two distinct subunits; they were found at different concentrations in several sugar cane tissues. It remains to be determined if the different gene expression levels have some physiological importance and how they affect sucrose synthesis, export, and storage in vacuoles. A comparison between the amino acid sequences of β PFKs from a variety of organisms allowed us to identify the two critical Asp residues typical of this enzyme's activity site and the other binding sites; these residues are tightly conserved in all members of this protein family. Apparently, there are catalytic residues on the β subunit of the pyrophosphate-dependent enzyme.
publishDate 2003
dc.date.none.fl_str_mv 2003-12-01
2014-05-27T11:20:59Z
2014-05-27T11:20:59Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.geneticsmr.com//year2003/vol2-4/pdf/gmr0065.pdf
Genetics and Molecular Research, v. 2, n. 4, p. 376-382, 2003.
1676-5680
http://hdl.handle.net/11449/67545
2-s2.0-2542463107
2-s2.0-2542463107.pdf
8951141172579985
7179273060624761
2663920223082171
url http://www.geneticsmr.com//year2003/vol2-4/pdf/gmr0065.pdf
http://hdl.handle.net/11449/67545
identifier_str_mv Genetics and Molecular Research, v. 2, n. 4, p. 376-382, 2003.
1676-5680
2-s2.0-2542463107
2-s2.0-2542463107.pdf
8951141172579985
7179273060624761
2663920223082171
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Genetics and Molecular Research
0,439
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 376-382
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808128894979538944