Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss
The Asr gene family is present in Spermatophyta. Its members are generally activated under water stress. We present evidence that tomato ASR1, one of the proteins of the family, accumulates in seed during late stages of embryogenesis, a physiological process characterized by water loss. In vitro, el...
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2007
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v352_n4_p831_Maskin http://hdl.handle.net/20.500.12110/paper_0006291X_v352_n4_p831_Maskin |
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paper:paper_0006291X_v352_n4_p831_Maskin2023-06-08T14:30:16Z Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss Maskin, Laura Frankel, Nicolás Gudesblat, Gustavo Eduardo Demergasso, María Julia Iusem, Norberto Daniel Asr genes Atomic force microscopy Dimerization Lycopersicon esculentum Seed dimer double stranded DNA homodimer monomer protein asr1 vegetable protein article atomic force microscopy chemical bond dimerization DNA binding electrophoresis embryo development gene activation hydrophilicity in vitro study multigene family nonhuman plant seed plant tissue priority journal protein assembly protein DNA interaction protein structure water loss Dimerization DNA-Binding Proteins Lycopersicon esculentum Microscopy, Atomic Force Plant Proteins Plasmids Protein Binding Seeds Water Lycopersicon esculentum Spermatophyta The Asr gene family is present in Spermatophyta. Its members are generally activated under water stress. We present evidence that tomato ASR1, one of the proteins of the family, accumulates in seed during late stages of embryogenesis, a physiological process characterized by water loss. In vitro, electrophoretic assays show a homo-dimeric structure for ASR1 and highlight strong non-covalent interactions between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) confirms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. © 2006 Elsevier Inc. All rights reserved. Fil:Maskin, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Frankel, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gudesblat, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Demergasso, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Iusem, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v352_n4_p831_Maskin http://hdl.handle.net/20.500.12110/paper_0006291X_v352_n4_p831_Maskin |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Asr genes Atomic force microscopy Dimerization Lycopersicon esculentum Seed dimer double stranded DNA homodimer monomer protein asr1 vegetable protein article atomic force microscopy chemical bond dimerization DNA binding electrophoresis embryo development gene activation hydrophilicity in vitro study multigene family nonhuman plant seed plant tissue priority journal protein assembly protein DNA interaction protein structure water loss Dimerization DNA-Binding Proteins Lycopersicon esculentum Microscopy, Atomic Force Plant Proteins Plasmids Protein Binding Seeds Water Lycopersicon esculentum Spermatophyta |
| spellingShingle |
Asr genes Atomic force microscopy Dimerization Lycopersicon esculentum Seed dimer double stranded DNA homodimer monomer protein asr1 vegetable protein article atomic force microscopy chemical bond dimerization DNA binding electrophoresis embryo development gene activation hydrophilicity in vitro study multigene family nonhuman plant seed plant tissue priority journal protein assembly protein DNA interaction protein structure water loss Dimerization DNA-Binding Proteins Lycopersicon esculentum Microscopy, Atomic Force Plant Proteins Plasmids Protein Binding Seeds Water Lycopersicon esculentum Spermatophyta Maskin, Laura Frankel, Nicolás Gudesblat, Gustavo Eduardo Demergasso, María Julia Iusem, Norberto Daniel Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| topic_facet |
Asr genes Atomic force microscopy Dimerization Lycopersicon esculentum Seed dimer double stranded DNA homodimer monomer protein asr1 vegetable protein article atomic force microscopy chemical bond dimerization DNA binding electrophoresis embryo development gene activation hydrophilicity in vitro study multigene family nonhuman plant seed plant tissue priority journal protein assembly protein DNA interaction protein structure water loss Dimerization DNA-Binding Proteins Lycopersicon esculentum Microscopy, Atomic Force Plant Proteins Plasmids Protein Binding Seeds Water Lycopersicon esculentum Spermatophyta |
| description |
The Asr gene family is present in Spermatophyta. Its members are generally activated under water stress. We present evidence that tomato ASR1, one of the proteins of the family, accumulates in seed during late stages of embryogenesis, a physiological process characterized by water loss. In vitro, electrophoretic assays show a homo-dimeric structure for ASR1 and highlight strong non-covalent interactions between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) confirms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. © 2006 Elsevier Inc. All rights reserved. |
| author |
Maskin, Laura Frankel, Nicolás Gudesblat, Gustavo Eduardo Demergasso, María Julia Iusem, Norberto Daniel |
| author_facet |
Maskin, Laura Frankel, Nicolás Gudesblat, Gustavo Eduardo Demergasso, María Julia Iusem, Norberto Daniel |
| author_sort |
Maskin, Laura |
| title |
Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| title_short |
Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| title_full |
Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| title_fullStr |
Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| title_full_unstemmed |
Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| title_sort |
dimerization and dna-binding of asr1, a small hydrophilic protein abundant in plant tissues suffering from water loss |
| publishDate |
2007 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v352_n4_p831_Maskin http://hdl.handle.net/20.500.12110/paper_0006291X_v352_n4_p831_Maskin |
| work_keys_str_mv |
AT maskinlaura dimerizationanddnabindingofasr1asmallhydrophilicproteinabundantinplanttissuessufferingfromwaterloss AT frankelnicolas dimerizationanddnabindingofasr1asmallhydrophilicproteinabundantinplanttissuessufferingfromwaterloss AT gudesblatgustavoeduardo dimerizationanddnabindingofasr1asmallhydrophilicproteinabundantinplanttissuessufferingfromwaterloss AT demergassomariajulia dimerizationanddnabindingofasr1asmallhydrophilicproteinabundantinplanttissuessufferingfromwaterloss AT iusemnorbertodaniel dimerizationanddnabindingofasr1asmallhydrophilicproteinabundantinplanttissuessufferingfromwaterloss |
| _version_ |
1768543352961105920 |