Single Crystals of the Photochemical Reaction Center from Rhodobacter sphaeroides Wild Type Strain 2.4.1 Analyzed by Polarized Light

1988 ◽  
pp. 27-32 ◽  
Author(s):  
Harry A. Frank ◽  
Shahriar S. Taremi ◽  
James R. Knox ◽  
Werner Mäntele
Keyword(s):  
Single Crystals ◽  
Reaction Center ◽  
Rhodobacter Sphaeroides ◽  
Photochemical Reaction ◽  
Type Strain ◽  
Wild Type Strain ◽  
Polarized Light ◽  
Wild Type

scholarly journals Nitrite and Nitrous Oxide Reductase Regulation by Nitrogen Oxides in Rhodobacter sphaeroides f. sp.denitrificans IL106

1999 ◽  
Vol 181 (19) ◽  
pp. 6028-6032 ◽  
Author(s):  
Monique Sabaty ◽  
Carole Schwintner ◽  
Sandrine Cahors ◽  
Pierre Richaud ◽  
Andre Verméglio
Keyword(s):  
Nitrous Oxide ◽  
Nitrate Reductase ◽  
Rhodobacter Sphaeroides ◽  
Type Strain ◽  
Biochemical Analysis ◽  
Wild Type Strain ◽  
Nitrous Oxide Reductase ◽  
Wild Type ◽  
Genes Encoding ◽  
Membrane Bound

ABSTRACT We have cloned the nap locus encoding the periplasmic nitrate reductase in Rhodobacter sphaeroides f. sp.denitrificans IL106. A mutant with this enzyme deleted is unable to grow under denitrifying conditions. Biochemical analysis of this mutant shows that in contrast to the wild-type strain, the level of synthesis of the nitrite and N2O reductases is not increased by the addition of nitrate. Growth under denitrifying conditions and induction of N oxide reductase synthesis are both restored by the presence of a plasmid containing the genes encoding the nitrate reductase. This demonstrates that R. sphaeroides f. sp. denitrificans IL106 does not possess an efficient membrane-bound nitrate reductase and that nitrate is not the direct inducer for the nitrite and N2O reductases in this species. In contrast, we show that nitrite induces the synthesis of the nitrate reductase.

Physiological Competence of Atrazine-Resistant Strains of the Photosynthetic BacteriumRhodobacter sphaeroides(Rhodospirillaceae)

Weed Science ◽  
1988 ◽  
Vol 36 (6) ◽  
pp. 703-706 ◽  
Author(s):  
Alfred E. Brown ◽  
Bryan Truelove ◽  
Claudia T. Highfill ◽  
Scott G. Smith
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Resistant Strain ◽  
Type Strain ◽  
Wild Type Strain ◽  
Photosynthetic Bacterium ◽  
Optimal Conditions ◽  
Wild Type ◽  
Culture Study ◽  
Resistant Strains ◽  
Two Parameters

Two parameters of physiological competence, rate of CO2fixation and intraspecific competitiveness, were determined for one or more atrazine-resistant isolates of the photosynthetic bacteriumRhodobacter sphaeroides. Measured over a 2-h period under optimal conditions, two of the resistant isolates fixed CO2at a greater rate than the atrazine-susceptible, wild-type organism. In a mixed culture study, an atrazine-resistant strain was able to grow and compete successfully with the susceptible, wild-type strain for at least 14 days.

scholarly journals The N Terminus of FliM Is Essential To Promote Flagellar Rotation in Rhodobacter sphaeroides

2001 ◽  
Vol 183 (10) ◽  
pp. 3142-3148 ◽  
Author(s):  
Sebastian Poggio ◽  
Aurora Osorio ◽  
Gabriel Corkidi ◽  
Georges Dreyfus ◽  
Laura Camarena
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Type Strain ◽  
Wild Type Strain ◽  
Complex Interaction ◽  
Swimming Behavior ◽  
Wild Type ◽  
N Terminus ◽  
Show Evidence ◽  
Flagellar Rotation

ABSTRACT FliM is part of the flagellar switch complex. Interaction of this protein with phospho-CheY (CheY-P) through its N terminus constitutes the main information relay point between the chemotactic system and the flagellum. In this work, we evaluated the role of the N terminus of FliM in the swimming behavior of Rhodobacter sphaeroides. Strains expressing the FliM protein with substitutions in residues previously reported in Escherichia coli as being important for interaction with CheY showed an increased stop frequency compared with wild-type cells. In accordance, we observed that R. sphaeroides cells expressing FliM lacking either the first 13 or 20 amino acids from the N terminus showed a stopped phenotype. We show evidence that FliMΔ13 and FliMΔ20 are stable proteins and that cells expressing them allow flagellin export at levels indistinguishable from those detected for the wild-type strain. These results suggest that the N-terminal region of FliM is required to promote swimming in this bacterium. The role of CheY in controlling flagellar rotation in this organism is discussed.

scholarly journals Topography of reaction center subunits in the membrane of the photosynthetic bacterium, rhodopseudomonas sphaeroides.

1982 ◽  
Vol 95 (1) ◽  
pp. 179-188 ◽  
Author(s):  
G E Valkirs ◽  
G Feher
Keyword(s):  
Electron Microscope ◽  
Reaction Center ◽  
Type Strain ◽  
Wild Type Strain ◽  
Photosynthetic Bacterium ◽  
Rhodopseudomonas Sphaeroides ◽  
Wild Type

The localization of the reaction center polypeptides (L, M, and H) in the membranes of both the wild-type, strain 2.4.1, and the carotenoidless mutant, R-26, of Rhodopseudomonas sphaeroides was determined by using affinity-purified antibodies specific for these proteins. Binding of the antibodies to reaction center subunits in spheroplasts was visualized in the electron microscope by immunoferritin labeling. The H and M subunits were labeled at both the cytoplasmic and the periplasmic surfaces of the membrane, whereas the L subunit was labeled only at the periplasmic surface of the membrane. Thus, the reaction center is asymmetrically oriented in the membrane with at least two subunits (H and M) spanning the membrane.

scholarly journals Oxygen Regulation of the ccoN Gene Encoding a Component of the cbb3 Oxidase inRhodobacter sphaeroides 2.4.1T: Involvement of the FnrL Protein

1998 ◽  
Vol 180 (8) ◽  
pp. 2228-2231 ◽  
Author(s):  
Nigel J. Mouncey ◽  
Samuel Kaplan
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Type Strain ◽  
Wild Type Strain ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Wild Type ◽  
Transcriptional Fusion ◽  
Gene Encoding ◽  
Genes Encoding ◽  
In The Wild

ABSTRACT The ccoNOQP gene cluster of Rhodobacter sphaeroides 2.4.1T encodes acbb 3 cytochrome oxidase which is utilized in oxygen-limited conditions for aerobic respiration. The β-galactosidase activity of accoN::lacZ transcriptional fusion was low under high (30%)-oxygen and anaerobic growth conditions. Maximal ccoN::lacZexpression was observed when the oxygen concentration was lowered to 2%. In an FnrL mutant,ccoN::lacZ expression was significantly lower than in the wild-type strain, suggesting that FnrL is a positive regulator of genes encoding thecbb 3 oxidase.

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