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Nucleic Acids Research, 2001, Vol. 29, No. 11 2244-2250
© 2001 Oxford University Press

DNA-binding specificity and dimerization of the DNA-binding domain of the PEND protein in the chloroplast envelope membrane

Naoki Sato* and Niji Ohta

Department of Molecular Biology, Faculty of Science, Saitama University, 255 Shimo-Ohkubo, Saitama, Saitama Prefecture 338-8570, Japan

The PEND protein is a DNA-binding protein in the inner envelope membrane of a developing chloroplast, which may anchor chloroplast nucleoids. Here we report the DNA-binding characteristics of the N-terminal basic region plus leucine zipper (bZIP)-like domain of the PEND protein that we call cbZIP domain. The basic region of the cbZIP domain diverges significantly from the basic region of known bZIP proteins that contain a bipartite nuclear localization signal. However, the cbZIP domain has the ability to dimerize in vitro. Selection of binding sites from a random sequence pool indicated that the cbZIP domain preferentially binds to a canonical sequence, TAAGAAGT. The binding site was also confirmed by gel mobility shift analysis using a representative binding site within the chloroplast DNA. These results suggest that the cbZIP domain is a unique DNA-binding domain of the chloroplast protein.

* To whom correspondence should be addressed. Tel: +81 48 858 3623; Fax: +81 48 858 3384; Email: naokisat{at}molbiol.saitama-u.ac.jp


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