Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (585K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (17)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sato, N.
Right arrow Articles by Ohta, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sato, N.
Right arrow Articles by Ohta, N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
H. S. Kim, B. O. Park, J. H. Yoo, M. S. Jung, S. M. Lee, H. J. Han, K. E. Kim, S. H. Kim, C. O. Lim, D.-J. Yun, et al.
Identification of a Calmodulin-binding NAC Protein as a Transcriptional Repressor in Arabidopsis
J. Biol. Chem., December 14, 2007; 282(50): 36292 - 36302.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Kodama and H. Sano
Evolution of a Basic Helix-Loop-Helix Protein from a Transcriptional Repressor to a Plastid-resident Regulatory Factor: INVOLVEMENT IN HYPERSENSITIVE CELL DEATH IN TOBACCO PLANTS
J. Biol. Chem., November 17, 2006; 281(46): 35369 - 35380.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
K. Terasawa and N. Sato
Visualization of Plastid Nucleoids In situ Using the PEND-GFP Fusion Protein
Plant Cell Physiol., April 1, 2005; 46(4): 649 - 660.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Sekine, T. Hase, and N. Sato
Reversible DNA Compaction by Sulfite Reductase Regulates Transcriptional Activity of Chloroplast Nucleoids
J. Biol. Chem., June 28, 2002; 277(27): 24399 - 24404.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.