Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1.

Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Research Abstract Details 

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Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Abstract Text:

Yong-Jin Kim,In-Jeong Ko,Jin-Mok Lee,Ho-Young Kang,Young Min Kim,Samuel Kaplan,Jeong-Il Oh,

In this study, the H303A mutant form of the cbb(3) oxidase (H303A oxidase), which has the H303A mutation in its catalytic subunit (CcoN), was purified from Rhodobacter sphaeroides. The H303A oxidase showed the same catalytic activity as did the wild-type form of the oxidase (WT oxidase). The heme contents of the mutant and WT forms of the cbb(3) oxidase were also comparable. However, the puf and puc operons, which are under the control of the PrrBA two-component system, were shown to be derepressed aerobically in the R. sphaeroides strain expressing the H303A oxidase. Since the strain harboring the H303A oxidase exhibited the same cytochrome c oxidase activity as the stain harboring the WT oxidase did, the aerobic derepression of photosynthesis gene expression observed in the H303A mutant appears to be the result of a defective signaling function of the H303A oxidase rather than reflecting any redox changes in the ubiquinone/ubiquinol pool. It was also demonstrated that ubiquinone inhibits not only the autokinase activity of full-length PrrB but also that of the truncated form of PrrB lacking its transmembrane domain, including the proposed quinone binding sequence. These results imply that the suggested ubiquinone binding site within the PrrB transmembrane domain is not necessary for the inhibition of PrrB kinase activity by ubiquinone. Instead, it is probable that signaling through H303 of the CcoN subunit of the cbb(3) oxidase is part of the pathway through which the cbb(3) oxidase affects the relative kinase/phosphatase activity of the membrane-bound PrrB.

Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Publishing Authors By Initials

YJ Kim,IJ Ko,JM Lee,HY Kang,YM Kim,S Kaplan,JI Oh,

For similar organic chemicals: quinones: benzoquinones: ubiquinone research abstracts see: organic chemicals: quinones: benzoquinones: ubiquinone research

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Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of bacteriology

VOLUME: 189

Page Numbers: 5617-25

Journal Abbreviation: J. Bacteriol.

ISSN: 0021-9193

DAY: 8

MONTH: 06

YEAR: 2007

Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985120

Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Keywords Mesh Terms:

KEYWORDS: Ubiquinone

MESH TERMS: metabolism

Chemical & Substance for Abstract: Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. Information

Substance Name: protein-histidine kinase

Registry Number: EC 2.7.3.-

Grant and Affiliation Information for Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1.

AFFILIATION: Department of Microbiology, Pusan National University, 30 Jangjeon-dong, Geumjeong-gu, 609-735 Busan, Korea.

Country: United States

AGENCY: United States NIGMS

GRANT: GM15590

ACRONYM: GM

MEDLINETA: J Bacteriol

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