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THE PLANT CELL, Vol 9, Issue 9 1673-1682, Copyright © 1997 by American Society of Plant Biologists
A Novel Protein with DNA Binding Activity from Tobacco Chloroplast Nucleoids
T. Nakano, S. Murakami, T. Shoji, S. Yoshida, Y. Yamada and F. Sato
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Kyoto 606-01, Japan
A 41-kD DNA binding protein with a basic pl was purified from chloroplast
nucleoids in photomixotrophically cultured tobacco cells, and its amino
acid sequence was determined. Using this sequence information, its cDNA
(CND41) was isolated, and its nucleotide sequence was determined. The
predicted amino acid sequence of CND41 has a transit peptide of 120 amino
acids and a mature protein of 382 amino acids. A distinctive
helix-turn-helix motif in the lysine-rich N-terminal region of the mature
protein and an aspartyl protease active site motif were predicted.
Expression of a series of truncated CND41 proteins in Escherichia coli
indicated that the lysine-rich region is essential for DNA binding and that
CND41 nonspecifically binds chloroplast DNA. Protein gel blot analyses
showed CND41 mainly in cells and/or tissues containing
nonphotosynthesizing, actively growing plastids. In addition, the
accumulation of chloroplast transcripts in these cells and/or tissues
(e.g., transcripts for QB binding protein of photosystem II [psbA] and
large subunit of ribulose bisphosphate carboxylase [rbcL]) was negatively
correlated with the accumulation of CND41. Analyses of cultured cells of
transgenic tobacco with reduced CND41 levels showed a higher level of
expression of chloroplast genes compared with that of the wild type. We
discuss the possible function of CND41 as a negative regulator of
chloroplast gene expression.
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