DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription factors invitro

DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription... Homeodomain-leucine zipper (HDZip) proteins constitute a large family of transcription factors apparently unique to plants. In this report we characterize the DNA-binding and dimerization preferences in vitro of class I HDZip proteins. Using gel-exclusion chromatography and in vitro protein binding assays we demonstrate that the HDZip class I protein ATHB5 forms a homodimeric complex in solution. Consistent with this finding we have demonstrated the sequence-specific interaction of ATHB5 with a 9 bp pseudopalindromic DNA sequence, CAATNATTG, composed of two half-sites overlapping at a central position, by use of a PCR-assisted binding-site selection assay and competitive EMSA experiments. A majority of other known members of HDZip class I interacted with similar DNA sequences, but differed in their preference for A/T versus G/C in the central position of the binding site. Selective heterodimerization in vitro was demonstrated between ATHB5 and different class I HDZip proteins. Heterodimer formation between class I HDZip proteins is of potential functional significance for the integration of information from different signalling pathways in the control of plant development. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription factors invitro

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Kluwer Academic Publishers
Copyright © 2001 by Kluwer Academic Publishers
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
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