Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss

doi:10.1016/j.bbrc.2006.11.115

Title: Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss

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Abstract

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.

Authors:

Maskin, Laura ^[1]; Frankel, Nicolas ^[1]; Gudesblat, Gustavo ^[1]; Demergasso, Maria J. ^[2]; Pietrasanta, Lia I. ^[2]; Iusem, Norberto D. ^[3]

Laboratorio de Fisiologia y Biologia Molecular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires (Argentina)
Centro de Microscopias Avanzadas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires (Argentina)
Laboratorio de Fisiologia y Biologia Molecular, IFIBYNE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires (Argentina). E-mail: norbius@fbmc.fcen.uba.ar

Publication Date:: Fri Jan 26 00:00:00 EST 2007

OSTI Identifier:: 20857969

Resource Type:: Journal Article

Resource Relation:: Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 352; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2006.11.115; PII: S0006-291X(06)02507-1; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; ATOMIC FORCE MICROSCOPY; DIMERIZATION; DIMERS; DNA; GENES; IN VITRO; MONOMERS; PLANT TISSUES; PROTEINS; SEEDS; TOMATOES

Citation Formats


                    Maskin, Laura, Frankel, Nicolas, Gudesblat, Gustavo, Demergasso, Maria J., Pietrasanta, Lia I., and Iusem, Norberto D.. Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss.  United States: N. p., 2007. 
        Web.  doi:10.1016/j.bbrc.2006.11.115.

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                    Maskin, Laura, Frankel, Nicolas, Gudesblat, Gustavo, Demergasso, Maria J., Pietrasanta, Lia I., & Iusem, Norberto D.. Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss.  United States.  doi:10.1016/j.bbrc.2006.11.115.

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                    Maskin, Laura, Frankel, Nicolas, Gudesblat, Gustavo, Demergasso, Maria J., Pietrasanta, Lia I., and Iusem, Norberto D.. Fri .  
        "Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss".  United States.  
        doi:10.1016/j.bbrc.2006.11.115.

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@article{osti_20857969,

  title        = {Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss},

  author       = {Maskin, Laura and Frankel, Nicolas and Gudesblat, Gustavo and Demergasso, Maria J. and Pietrasanta, Lia I. and Iusem, Norberto D.},

  abstractNote = {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.},

  doi          = {10.1016/j.bbrc.2006.11.115},

  journal      = {Biochemical and Biophysical Research Communications},

  number       = 4,

  volume       = 352,

  place        = {United States},

  year         = {Fri Jan 26 00:00:00 EST 2007},

  month        = {Fri Jan 26 00:00:00 EST 2007}

}

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DOI: 10.1016/j.bbrc.2006.11.115

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