The water- and salt-stress-regulated Asr1 (abscisic acid stress ripening) gene encodes a zinc-dependent DNA-binding protein

Tomato (Lycopersicon esculantum) ASR1 (abscisic acid stress ripening protein), a small plant-specific protein whose cellular mode of action defies deduction based on its sequence or homology analyses, is one of numerous plant gene products with unknown biological roles that become over-expressed und...

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Published inBiochemical journal Vol. 381; no. Pt 2; pp. 373 - 378
Main Authors Kalifa, Yossi, Gilad, Ayelet, Konrad, Zvia, Zaccai, Michele, Scolnik, Pablo A, Bar-Zvi, Dudy
Format Journal Article
LanguageEnglish
Published England Portland Press Ltd 15.07.2004
Subjects
Binding Sites - genetics
Cell Fractionation - methods
DNA, Plant - genetics
DNA-Binding Proteins - genetics
Escherichia coli
Gene Expression Regulation, Plant - genetics
Lycopersicon
Lycopersicon esculentum
Plant Proteins - genetics
Plant Proteins - metabolism
Sodium Chloride - metabolism
Solanum lycopersicum - cytology
Solanum lycopersicum - genetics
Subcellular Fractions - chemistry
Water - metabolism
Zinc Fingers - genetics
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Summary:Tomato (Lycopersicon esculantum) ASR1 (abscisic acid stress ripening protein), a small plant-specific protein whose cellular mode of action defies deduction based on its sequence or homology analyses, is one of numerous plant gene products with unknown biological roles that become over-expressed under water- and salt-stress conditions. Steady-state cellular levels of tomato ASR1 mRNA and protein are transiently increased following exposure of plants to poly(ethylene glycol), NaCl or abscisic acid. Western blot and indirect immunofluorescence analysis with anti-ASR1 antibodies demonstrated that ASR1 is present both in the cytoplasmic and nuclear subcellular compartments; approx. one-third of the total ASR1 protein could be detected in the nucleus. Nuclear ASR1 is a chromatin-bound protein, and can be extracted with 1 M NaCl, but not with 0.5% Triton X-100. ASR1, overexpressed in Escherichia coli and purified to homogeneity, possesses zinc-dependent DNA-binding activity. Competitive-binding experiments and SELEX (systematic evolution of ligands by exponential enrichment) analysis suggest that ASR1 binds at a preferred DNA sequence.
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1These authors contributed equally to this work.
2Present address: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, U.S.A.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj20031800