Identification and characterization of GIP1, anArabidopsis thaliana protein that enhances the DNA binding affinity and reduces the oligomeric state of G-box binding factors

Paul C. SEHNKE; Beth J. LAUGHNER; Carla R. LYERLY LINEBARGERWilliam B. GURLEYRobert J. FERL

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Identification and characterization of GIP1, anArabidopsis thaliana protein that enhances the DNA binding affinity and reduces the oligomeric state of G-box binding factors

机译：Identification and characterization of GIP1, anArabidopsis thaliana protein that enhances the DNA binding affinity and reduces the oligomeric state of G-box binding factors

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Environmental control of the alcohol dehydrogenase (Adh) and other stress response genes in plants is in part brought about by transcriptional regulation involving the G-box cis-acting DNA element and bZIP G-box Binding Factors (GBFs). The mechanismsof GBF regulation and requirements for additional factors in this control process are not well understood. In an effort to identify potential GBF binding and control partners, maize GBF1 was used as bait in a yeast two-hybrid screen of an A. thaliana cDNA library. GBF Interacting Protein 1 (GIP1) arose from the screen as a 496 amino acid protein with a predicted molecular weight of 53,748 kDa that strongly interacts with GBFs. Northern analysis of A. thaliana tissue suggests a 1.8-1.9 kb GIP1 transcript, predominantly in roots. Immunolocalization studies indicate that GIP1 protein is mainly localized to the nucleus. In vitro electrophoretic mobility shift assays using an Adh G-box DNA probe and recombinant A. thaliana GBFS or maize GBF1, showed that the presence of GIP1 resulted in a tenfold increase in GBF DNA binding activity without altering the migration, suggesting a transient association between GIP1 and GBF. Addition of GIP1 to intentionally aggregated GBF converted GBF to lower molecular weight macromolecular complexes and GIP1 also refolded denatured rhodanese in the absence of ATP. These data suggest GIP1 functions to enhance GBF DNA binding activity by acting as a potent nuclear chaperone or crowbar, and potentially regulates the multimeric state of GBFs, thereby contributing to bZIP-mediated gene regulation.

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《Cell research》 |2005年第8期|567-575|共9页
作者
Paul C. SEHNKE; Beth J. LAUGHNER; Carla R. LYERLY LINEBARGERWilliam B. GURLEYRobert J. FERL;
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作者单位

Program in Plant Cellular and Molecular Biology, Department of Horticultural Sciences, University of Florida, Gainesville, FL 32611, USA;

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收录信息美国《科学引文索引》(SCI);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类细胞生物学;
关键词
G-box binding factor interacting protein; nuclear chaperone; DNA binding affinity;

Identification and characterization of GIP1, anArabidopsis thaliana protein that enhances the DNA binding affinity and reduces the oligomeric state of G-box binding factors

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