Abstract
The INDETERMINATE protein, ID1, plays a key role in regulating the floral transition in maize. ID1 is the founding member of a plant-specific zinc finger protein family that is defined by a highly conserved amino acid sequence called ID domain. The ID domain includes a cluster of three different type of zinc fingers separated from a canonical C2H2 finger by a long spacer; ID is distinct from other ID family proteins by having a much longer spacer.
We determined the binding sequence of ID1 by in vitroDNA selection and amplification binding assays and analyzed the DNA binding properties of ID1 and ID family proteins. Our results demonstrate that maize ID1 and ID family proteins have novel zinc finger configurations with unique DNA binding properties.
