Dimerization and DNA-binding of ASR1, a small hydrophilic protein abundant in plant tissues suffering from water loss
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:
- 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:
- 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.
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.
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.
@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}
}
Other availability
Save to My Library
You must Sign In or Create an Account in order to save documents to your library.
-
Abundant constitutive expression of the immediate-early 94K protein from cytomegalovirus (Colburn) in a DNA-transfected mouse cell line
A 94-kilodalton phosphoprotein known as IE94 is the only viral polypeptide synthesized in abundance under immediate-early conditions after infection by cytomegalovirus (CMV) strain Colburn in either permissive primate or nonpermissive rodent cells. The authors isolated a clonal Ltk/sup +/ cell line which expressed the /sup 35/methionine-labeled IE94 polypeptide in sufficient abundance to be visualized directly in autoradiographs after gel electrophoresis of total-cell-culture protein extracts. The IE94 polypeptide synthesized in the transfected cells was indistinguishable in size and overall net charge from that produced in virus-infected cells. In addition, the IE94 protein expressed in LH/sub 2/p198-3 cells was phosphorylated (presumably bymore »