Journal article

Publication year: 1991

Pages: 167-176

Journal: Molecular and General Genetics MGG

Volume number: 226

Issue number: 1-2

ISSN: 0026-8925

DOI Link: https://doi.org/10.1007/BF00273600

Publisher: Springer Verlag (Germany)

Abstract: 
The transcription of the polycistronic puf operon which encodes pigment binding proteins of the reaction center and light-harvesting complex I of Rhodobacter capsulatus is regulated by the oxygen tension in the culture. A DNA sequence upstream of the puf transcriptional start was identified as a protein binding site. A DNA fragment carrying this DNA sequence participated in the formation of two DNA-protein complexes. The relative amounts of the two complexes were dependent on the oxygen tension in cultures from which the cytosolic fraction used for the in vitro binding studies was isolated. A single base pair transition within the protein binding site affected the oxygen-dependent expression of puf in vivo and the formation of DNA-protein complexes in vitro. The data suggest that the formation of specific DNA-protein complexes is involved in the oxygen-dependent regulation of the puf promoter. A DNA fragment containing the promoter region of the puc operon that encodes proteins of the light-harvesting complex II acted as a competitor for the formation of the DNA-protein complexes with the puf-specific fragment, indicating coregulation of the two operons.

Harvard Citation style: Klug, G. (1991) A DNA sequence upstream of the puf operon of Rhodobacter capsulatus is involved in its oxygen-dependent regulation and functions as a protein binding site, Molecular and General Genetics MGG, 226(1-2), pp. 167-176. https://doi.org/10.1007/BF00273600

APA Citation style: Klug, G. (1991). A DNA sequence upstream of the puf operon of Rhodobacter capsulatus is involved in its oxygen-dependent regulation and functions as a protein binding site. Molecular and General Genetics MGG. 226(1-2), 167-176. https://doi.org/10.1007/BF00273600