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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Autores principales: Maskin, L., Frankel, N., Gudesblat, G., Demergasso, M.J., Pietrasanta, L.I., Iusem, N.D.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v352_n4_p831_Maskin
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spelling todo:paper_0006291X_v352_n4_p831_Maskin2023-10-03T14:03:52Z Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss Maskin, L. Frankel, N. Gudesblat, G. Demergasso, M.J. Pietrasanta, L.I. Iusem, N.D. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, L.
Frankel, N.
Gudesblat, G.
Demergasso, M.J.
Pietrasanta, L.I.
Iusem, N.D.
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.
format JOUR
author Maskin, L.
Frankel, N.
Gudesblat, G.
Demergasso, M.J.
Pietrasanta, L.I.
Iusem, N.D.
author_facet Maskin, L.
Frankel, N.
Gudesblat, G.
Demergasso, M.J.
Pietrasanta, L.I.
Iusem, N.D.
author_sort Maskin, L.
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
url http://hdl.handle.net/20.500.12110/paper_0006291X_v352_n4_p831_Maskin
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