Journalartikel

Jahr der Veröffentlichung: 2000

Seiten: 235-243

Zeitschrift: Journal of Molecular Microbiology and Biotechnology

Bandnummer: 2

Heftnummer: 2

ISSN: 1464-1801

URL: https://www.caister.com/jmmb/v/v2/v2n2/11.pdf

Verlag: Karger Publishers

Abstract: 
The transcription of genes encoding pigment binding proteins in the facultative photosynthetic bacterium Rhodobacter capsulatus is regulated in response to oxygen partial pressure. Previous results identified RegA and RegB as members of a two component system involved in oxygen dependent synthesis of the photosynthetic apparatus. Here we demonstrate that RegA differentially controls the transcription of the puf and puc operons which encode proteins of the LHI and LHII antenna complexes, respectively. In a regA mutant strain the level of puf specific mRNA reaches about 30% of the wild type levels and transcription is still responsive to oxygen tension. In contrast, the level of puc specific mRNA is very low and is no longer oxygen regulated. RegA binds to DNA sequences upstream of both the puf and puc operons, although with different affinities. We provide experimental evidence that a putative helix-turn-helix motif in the C-terminal region of RegA is responsible for its specific binding to the puf and puc promoter regions. In contrast to many other response regulators, the affinity of RegA for the target DNA is only slightly modified by phosphorylation.

Harvard-Zitierstil: Hemschemeier, S., Kirndorfer, M., Hebermehl, M. and Klug, G. (2000) DNA binding of wild type RegA protein and its differential effect on the expresion of pigment binding proteins in Rhodobacter capsulatus, Journal of Molecular Microbiology and Biotechnology, 2(2), pp. 235-243. https://www.caister.com/jmmb/v/v2/v2n2/11.pdf

APA-Zitierstil: Hemschemeier, S., Kirndorfer, M., Hebermehl, M., & Klug, G. (2000). DNA binding of wild type RegA protein and its differential effect on the expresion of pigment binding proteins in Rhodobacter capsulatus. Journal of Molecular Microbiology and Biotechnology. 2(2), 235-243. https://www.caister.com/jmmb/v/v2/v2n2/11.pdf