1IRZ

Solution structure of ARR10-B belonging to the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators

Summary for 1IRZ

• Entry DOI: 10.2210/pdb1irz/pdb
• NMR Information: BMRB: 5174
• Descriptor: ARR10-B (1 entity in total)
• Functional Keywords: helix-turn-helix, dna binding protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Nucleus: O49397
• Total number of polymer chains: 1
• Total formula weight: 7384.76

Authors

Yamazaki, T.,Katoh, E.,Hosoda, K.,Mizuno, T. (deposition date: 2001-10-25, release date: 2003-02-11, Last modification date: 2023-12-27)

Primary citation

Hosoda, K.,Imamura, A.,Katoh, E.,Hatta, T.,Tachiki, M.,Yamada, H.,Mizuno, T.,Yamazaki, T.
Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators
PLANT CELL, 14:2015-2029, 2003

PubMed Abstract: The B motif is a signature of type-B response regulators (ARRs) involved in His-to-Asp phosphorelay signal transduction systems in Arabidopsis. Homologous motifs occur widely in the GARP family of plant transcription factors. To gain general insight into the structure and function of B motifs (or GARP motifs), we characterized the B motif derived from a representative ARR, ARR10, which led to a number of intriguing findings. First, the B motif of ARR10 (named ARR10-B and extending from Thr-179 to Ser-242) possesses a nuclear localization signal, as indicated by the intracellular localization of a green fluorescent protein-ARR10-B fusion protein in onion epidermal cells. Second, the purified ARR10-B molecule binds specifically in vitro to DNA with the core sequence AGATT. This was demonstrated by several in vitro approaches, including PCR-assisted DNA binding site selection, gel retardation assays, and surface plasmon resonance analysis. Finally, the three-dimensional structure of ARR10-B in solution was determined by NMR spectroscopy, showing that it contains a helix-turn-helix structure. Furthermore, the mode of interaction between ARR10-B and the target DNA was assessed extensively by NMR spectroscopy. Together, these results lead us to propose that the mechanism of DNA recognition by ARR10-B is essentially the same as that of homeodomains. We conclude that the B motif is a multifunctional domain responsible for both nuclear localization and DNA binding and suggest that these insights could be applicable generally to the large GARP family of plant transcription factors.

PubMed: 12215502
DOI: 10.1105/tpc.002733

Experimental method

SOLUTION NMR