TITLE

A Transcription Factor with a Leucine-Zipper Motif Involved in Light-Dependent Inhibition of Expression of the puf Operon in the Photosynthetic Bacterium Rhodobacter sphaeroides

AUTHOR(S)
Shimada, Hiroshi; Wada, Tadashi; Handa, Hiroshi; Ohta, Hiroyuki; Mizoguchi, Hiroshi; Nishimura, Kohji; Masuda, Tatsuru; Shioi, Yuzo; Takamiya, Ken-ichiro
PUB. DATE
June 1996
SOURCE
Plant & Cell Physiology;Jun1996, Vol. 37 Issue 4, p515
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
In the purple nonsulfur photosynthetic bacterium Rhodobacter sphaeroides the synthesis of components of the photosystem is regulated in response to oxygen tension and light intensity. We have purified and cloned a trans-acting protein (SPB) that binds to the promoter region of the puf operon, which encodes the apoproteins of light-harvesting complex I and the reaction center. The SPB was composed of a single polypeptide with an apparent molecular mass of 15.0 kDa. The nucleotide sequence of the spb gene was determined. The gene encoded 104 amino acid residues, which correspond to a molecular mass of 11.5 kDa. SPB exhibited 53% homology to HvrA in Rhodobacter capsulatus. The deduced amino acid sequence indicated that SPB contained a region with homology to the leucinezipper motif of c-JUN, a transcription factor in eukaryotes, and SPB also had a DNA-binding domain on the amino-terminal side of the leucine-zipper motif. The leucine-zipper motif of SPB might contribute to the formation of a dimer. Northern analysis indicated that spb was constitutively and monocistronically transcribed in R. sphaeroides, irrespective of growth conditions. Structural and functional differences between SPB and HvrA are discussed.
ACCESSION #
79306810

 

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics