Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.

A thermolabile UPTG inhibitor protein (IP) was isolated and purified from a developing maize endosperm preparation. High homology of two internal peptides of IP with known plant sucrose synthase (SS) sequences suggested that IP might be related somehow with SS. IP and SS activities were found in the...

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Autores principales: Wald, F.A., Rothschild, A., Moreno, S., Tandecarz, J.S.
Formato: JOUR
Materias:
alpha 1,4 glucan protein synthase (UDP forming)
alpha-1,4-glucan-protein synthase (UDP-forming)
enzyme inhibitor
glucosyltransferase
sucrose synthase
vegetable protein
amino acid sequence
article
chemistry
drug antagonism
isolation and purification
maize
molecular genetics
sequence homology
serodiagnosis
Amino Acid Sequence
Enzyme Inhibitors
Glucosyltransferases
Molecular Sequence Data
Neutralization Tests
Plant Proteins
Sequence Homology, Amino Acid
Zea mays
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p397_Wald
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_01455680_v44_n3_p397_Wald
record_format dspace
spelling todo:paper_01455680_v44_n3_p397_Wald2023-10-03T14:59:59Z Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein. Wald, F.A. Rothschild, A. Moreno, S. Tandecarz, J.S. alpha 1,4 glucan protein synthase (UDP forming) alpha-1,4-glucan-protein synthase (UDP-forming) enzyme inhibitor glucosyltransferase sucrose synthase vegetable protein amino acid sequence article chemistry drug antagonism isolation and purification maize molecular genetics sequence homology serodiagnosis Amino Acid Sequence Enzyme Inhibitors Glucosyltransferases Molecular Sequence Data Neutralization Tests Plant Proteins Sequence Homology, Amino Acid Zea mays A thermolabile UPTG inhibitor protein (IP) was isolated and purified from a developing maize endosperm preparation. High homology of two internal peptides of IP with known plant sucrose synthase (SS) sequences suggested that IP might be related somehow with SS. IP and SS activities were found in the same preparation and showed thermolability between 60-65 degrees C. IP and SS activities presented the same ionic charge and molecular mass in native conditions (Mono Q and Superose-12 columns chromatographies). Western blot experiments with an anti-SS antibody as well as with an anti-IP antibody showed a single 80 kDa polypeptide band where IP and SS activities were present. Anti-SS antibody can neutralize SS as well as IP activities in a neutralization assay. It was found that in the maize mutant shrunken-1, lacking SS1 protein, the UPTG activity was not inhibited. Furthermore, the solubilized preparation of the sh1 endosperm is unable of inhibiting UPTG activity from potato tuber. The high correlation between IP and SS properties suggests that IP might be in fact a form of SS. Moreover, the relation between IP and the SS1 isoform is discussed. So, a new biological activity of SS is suggested. Fil:Wald, F.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Rothschild, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Tandecarz, J.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p397_Wald
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic alpha 1,4 glucan protein synthase (UDP forming)
alpha-1,4-glucan-protein synthase (UDP-forming)
enzyme inhibitor
glucosyltransferase
sucrose synthase
vegetable protein
amino acid sequence
article
chemistry
drug antagonism
isolation and purification
maize
molecular genetics
sequence homology
serodiagnosis
Amino Acid Sequence
Enzyme Inhibitors
Glucosyltransferases
Molecular Sequence Data
Neutralization Tests
Plant Proteins
Sequence Homology, Amino Acid
Zea mays
spellingShingle alpha 1,4 glucan protein synthase (UDP forming)
alpha-1,4-glucan-protein synthase (UDP-forming)
enzyme inhibitor
glucosyltransferase
sucrose synthase
vegetable protein
amino acid sequence
article
chemistry
drug antagonism
isolation and purification
maize
molecular genetics
sequence homology
serodiagnosis
Amino Acid Sequence
Enzyme Inhibitors
Glucosyltransferases
Molecular Sequence Data
Neutralization Tests
Plant Proteins
Sequence Homology, Amino Acid
Zea mays
Wald, F.A.
Rothschild, A.
Moreno, S.
Tandecarz, J.S.
Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
topic_facet alpha 1,4 glucan protein synthase (UDP forming)
alpha-1,4-glucan-protein synthase (UDP-forming)
enzyme inhibitor
glucosyltransferase
sucrose synthase
vegetable protein
amino acid sequence
article
chemistry
drug antagonism
isolation and purification
maize
molecular genetics
sequence homology
serodiagnosis
Amino Acid Sequence
Enzyme Inhibitors
Glucosyltransferases
Molecular Sequence Data
Neutralization Tests
Plant Proteins
Sequence Homology, Amino Acid
Zea mays
description A thermolabile UPTG inhibitor protein (IP) was isolated and purified from a developing maize endosperm preparation. High homology of two internal peptides of IP with known plant sucrose synthase (SS) sequences suggested that IP might be related somehow with SS. IP and SS activities were found in the same preparation and showed thermolability between 60-65 degrees C. IP and SS activities presented the same ionic charge and molecular mass in native conditions (Mono Q and Superose-12 columns chromatographies). Western blot experiments with an anti-SS antibody as well as with an anti-IP antibody showed a single 80 kDa polypeptide band where IP and SS activities were present. Anti-SS antibody can neutralize SS as well as IP activities in a neutralization assay. It was found that in the maize mutant shrunken-1, lacking SS1 protein, the UPTG activity was not inhibited. Furthermore, the solubilized preparation of the sh1 endosperm is unable of inhibiting UPTG activity from potato tuber. The high correlation between IP and SS properties suggests that IP might be in fact a form of SS. Moreover, the relation between IP and the SS1 isoform is discussed. So, a new biological activity of SS is suggested.
format JOUR
author Wald, F.A.
Rothschild, A.
Moreno, S.
Tandecarz, J.S.
author_facet Wald, F.A.
Rothschild, A.
Moreno, S.
Tandecarz, J.S.
author_sort Wald, F.A.
title Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
title_short Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
title_full Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
title_fullStr Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
title_full_unstemmed Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
title_sort identification of a uptg inhibitor protein from maize endosperm: high homology with sucrose synthase protein.
url http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p397_Wald
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AT rothschilda identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein
AT morenos identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein
AT tandecarzjs identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein
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