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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1998
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p397_Wald http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p397_Wald |
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paper:paper_01455680_v44_n3_p397_Wald2023-06-08T15:12:22Z Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein. Wald, Flavia A. Rothschild, Andrea Moreno de Colonna, Silvia Tandecarz, Juana Sara 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. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p397_Wald 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, Flavia A. Rothschild, Andrea Moreno de Colonna, Silvia Tandecarz, Juana Sara 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. |
| author |
Wald, Flavia A. Rothschild, Andrea Moreno de Colonna, Silvia Tandecarz, Juana Sara |
| author_facet |
Wald, Flavia A. Rothschild, Andrea Moreno de Colonna, Silvia Tandecarz, Juana Sara |
| author_sort |
Wald, Flavia 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. |
| publishDate |
1998 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p397_Wald http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p397_Wald |
| work_keys_str_mv |
AT waldflaviaa identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein AT rothschildandrea identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein AT morenodecolonnasilvia identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein AT tandecarzjuanasara identificationofauptginhibitorproteinfrommaizeendospermhighhomologywithsucrosesynthaseprotein |
| _version_ |
1768544772639686656 |