Dimerization and DNA-binding of ASR1, a small hydrophilic

LAURA MASKIN; NICOLÁS FRANKEL; GUSTAVO GUDESBLAT; MARÍA J. DEMERGASSO; LÍA I. PIETRSANTA; NORBERTO D. IUSEM

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Elsevier

Lugar: Amsterdam; Año: 2007 vol. 352 p. 831 - 835

0006-291X

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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. between monomers prone to self-assemble. Direct visualization of single molecules by atomic force microscopy (AFM) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA. 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) con.rms that ASR1 forms homodimers and that uncovers both monomers and dimers bind double stranded DNA.