The role of cysteine 160 in thiamine diphosphate binding of the Calvin–Benson–Bassham cycle transketolase of Rhodobacter sphaeroides

2004 ◽  
Vol 426 (1) ◽  
pp. 43-54 ◽  
Author(s):  
Cedric E Bobst ◽  
F.Robert Tabita
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Thiamine Diphosphate

scholarly journals Genetic and Phenotypic Analyses of therdx Locus of Rhodobacter sphaeroides2.4.1

2000 ◽  
Vol 182 (12) ◽  
pp. 3475-3481 ◽  
Author(s):  
Jung Hyeob Roh ◽  
Samuel Kaplan
Keyword(s):  
Gene Expression ◽  
Rhodobacter Sphaeroides ◽  
Redox Protein ◽  
Deletion Mutations ◽  
Metal Transporter ◽  
New Class ◽  
Mutant Strains ◽  
Membrane Bound ◽  
Photosynthesis Gene

ABSTRACT Previously, we reported that rdxB, encoding a likely membrane-bound two [4Fe-4S]-containing center, is involved in the aerobic regulation of photosystem gene expression in Rhodobacter sphaeroides 2.4.1. To further investigate the role ofrdxB as well as other genes of the rdxBHISoperon on photosystem gene expression, we constructed a series of nonpolar, in-frame deletion mutations in each of the rdxgenes. Using both puc and puf operonlacZ fusions to monitor photosystem gene expression, under aerobic conditions, in each of the mutant strains revealed significant increased photosynthesis gene expression. In the case of mutations in either rdxH, rdxI, or rdxS, the aerobic induction of photosystem gene expression is believed to be indirect by virtue of a posttranscriptional effect oncbb 3 cytochrome oxidase structure and integrity. For RdxB, we suggest that this redox protein has a more direct effect on photosystem gene expression by virtue of its interaction with the cbb 3 oxidase. An associated phenotype, involving the enhanced conversion of the carotenoid spheroidene to spheroidenone, is also observed in the RdxB, -H, -I, and -S mutant strains. This phenotype is also suggested to be the result of the role of the rdxBHIS locus incbb 3 oxidase activity and/or structure. RdxI is suggested to be a new class of metal transporter of the CPx-type ATPases.

scholarly journals Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: the role of PufX

2004 ◽  
Vol 23 (4) ◽  
pp. 690-700 ◽  
Author(s):  
C Alistair Siebert ◽  
Pu Qian ◽  
Dimitrios Fotiadis ◽  
Andreas Engel ◽  
C Neil Hunter ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Molecular Architecture ◽  
Photosynthetic Membranes

Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone/ubiquinol exchange between the reaction center QB site and the cytochrome bc1 complex.

Biochemistry ◽  
1995 ◽  
Vol 34 (46) ◽  
pp. 15248-15258 ◽  
Author(s):  
Wolfgang P. Barz ◽  
Andre Vermeglio ◽  
Francesco Francia ◽  
Giovanni Venturoli ◽  
B. Andrea Melandri ◽  
...  
Keyword(s):  
Reaction Center ◽  
Rhodobacter Sphaeroides ◽  
Cytochrome Bc1 ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex

scholarly journals On the role of the light-harvesting B880 in the correct insertion of the reaction center of Rhodobacter capsulatus and Rhodobacter sphaeroides

FEBS Letters ◽  
1987 ◽  
Vol 215 (1) ◽  
pp. 171-174 ◽  
Author(s):  
W.Jim Jackson ◽  
Patricia J. Kiley ◽  
Copper E. Haith ◽  
Samuel Kaplan ◽  
Roger C. Prince
Keyword(s):  
Reaction Center ◽  
Rhodobacter Sphaeroides ◽  
Rhodobacter Capsulatus ◽  
Light Harvesting

scholarly journals Role of the Global Transcriptional Regulator PrrA in Rhodobacter sphaeroides 2.4.1: Combined Transcriptome and Proteome Analysis

2008 ◽  
Vol 190 (14) ◽  
pp. 4831-4848 ◽  
Author(s):  
Jesus M. Eraso ◽  
Jung Hyeob Roh ◽  
Xiaohua Zeng ◽  
Stephen J. Callister ◽  
Mary S. Lipton ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Regulatory System ◽  
Proteome Analysis ◽  
Orthologous Group ◽  
Transcriptional Level ◽  
Chromatographic Study ◽  
Metabolic Genes ◽  
Genes Encoding ◽  
Parameter Values

ABSTRACTThe PrrBA two-component regulatory system is a major global regulator inRhodobacter sphaeroides2.4.1. Here we have compared the transcriptome and proteome profiles of the wild-type (WT) and mutant PrrA2 cells grown anaerobically in the dark with dimethyl sulfoxide as an electron acceptor. Approximately 25% of the genes present in the PrrA2 genome are regulated by PrrA at the transcriptional level, either directly or indirectly, by twofold or more relative to the WT. The genes affected are widespread throughout all COG (cluster of orthologous group) functional categories, with previously unsuspected “metabolic” genes affected in PrrA2 cells. PrrA was found to act as both an activator and a repressor of transcription, with more genes being repressed in the presence of PrrA (9:5 ratio). An analysis of the genes encoding the 1,536 peptides detected through our chromatographic study, which corresponds to 36% coverage of the genome, revealed that approximately 20% of the genes encoding these proteins were positively regulated, whereas approximately 32% were negatively regulated by PrrA, which is in excellent agreement with the percentages obtained for the whole-genome transcriptome profile. In addition, comparison of the transcriptome and proteome mean parameter values for WT and PrrA2 cells showed good qualitative agreement, indicating that transcript regulation paralleled the corresponding protein abundance, although not one for one. The microarray analysis was validated by direct mRNA measurement of randomly selected genes that were both positively and negatively regulated.lacZtranscriptional andkantranslational fusions enabled us to map putative PrrA binding sites and revealed potential gene targets for indirect regulation by PrrA.

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