Succinate dehydrogenase--a comparative review.

Hederstedt, Lars; Rutberg, Lars

doi:10.1128/mmbr.45.4.542-555.1981

Cited by 88 publications

(44 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The relative abundances of succinate dehydrogenase subunits in UPB and ICM are similar within 1 SD, as expected for components of the same complex; the two other (membrane-intrinsic) subunits were not detected. The enrichment in ICM of succinate dehydrogenase, a component of the tricarboxylic acid cycle is unexpected, given that succinate dehydrogenase has often been used as a marker for CMs (Hederstedt and Rutberg, 1981). However, this finding may be rationalized by evidence that succinate dehydrogenase is active in the control of electron flow in cyanobacterial thylakoid membranes (Cooley and Vermaas, 2001).…”

Section: Energy Transduction: Proteins That Mediate Electron Transpormentioning

confidence: 99%

Quantitative proteomic analysis of intracytoplasmic membrane development in Rhodobacter sphaeroides

Jackson

Lewis

Tucker

et al. 2012

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe purple phototrophic bacteria elaborate a specialized intracytoplasmic membrane (ICM) system for the conversion of solar energy to ATP. Previous radiolabelling and ultrastructural experiments have shown that ICM assembly in Rhodobacter sphaeroides is initiated at indentations of the cytoplasmic membrane, termed UPB. Here, we report proteomic analyses of precursor (UPB) and mature (ICM) fractions. Qualitative data identified 387 proteins, only 43 of which were found in the ICM, reflecting its specialized role within the cell, the conversion of light into chemical energy; 236 proteins were found in the significantly more complex UPB proteome. Metabolic labelling was used to quantify the relative distribution of 173 proteins between the UPB and ICM fractions. Quantification reveals new information on assembly of the RC-LH1-PufX, ATP synthase and NAD(P)H transhydrogenase complexes, as well as showing that the UPB is enriched in enzymes for lipid, carbohydrate and amino acid metabolism, tetrapyrrole biosynthesis and proteins representing a wide range of other metabolic and biosynthetic functions. Proteins involved in light harvesting, photochemistry, electron transport and ATP synthesis are all enriched in ICM, consistent with the spatial proximity of energy capturing and transducing functions. These data provide further support to the developmental precursor-product relationship between UPB and ICM.

show abstract

Section: Energy Transduction: Proteins That Mediate Electron Transpormentioning

confidence: 99%

Quantitative proteomic analysis of intracytoplasmic membrane development in Rhodobacter sphaeroides

Jackson

Lewis

Tucker

et al. 2012

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…However, other upregulated genes would be in agreement with a pathway involving succinate as an intermediate. The significantly upregulated SPO0361 is a succinate dehydrogenase (EC 1.3.99.1), a well-known TCA cycle enzyme that converts succinate to fumarate (Hederstedt and Rutberg, 1981). Some genes for intermediate steps, such as acyl-CoA dehydrogenase-like genes for the conversion of acryloyl-CoA to propionyl-CoA (SPO3804, SPO0693, SPO1968, SPO0879, SPOA0288) and methylmalonyl-CoA epimerase (SPO0932) for the conversion of (S)-methylmalonyl-CoA to (R)methylmalonyl-CoA are among potentially upregulated genes.…”

Section: Putative Propionate Moiety Degradation Genesmentioning

confidence: 99%

Transcriptional response of Silicibacter pomeroyi DSS‐3 to dimethylsulfoniopropionate (DMSP)

Bürgmann¹,

Howard

Ye³

et al. 2007

Environmental Microbiology

View full text Add to dashboard Cite

Dimethylsufoniopropionate (DMSP) is an abundant organic sulfur compound in the ocean and an important substrate for marine bacterioplankton. The Roseobacter clade of marine alphaproteobacteria, including Silicibacter pomeroyi strain DSS-3, are known to be involved in DMSP degradation in situ. The fate of DMSP has important implications for the global sulfur cycle, but the genes involved in this process and their regulation are largely unknown. S. pomeroyi is capable of performing two major pathways of DMSP degradation, making it an important model organism. Based on the full genome sequence of this strain we designed an oligonucleotide-based microarray for the detection of transcripts of nearly all genes. The array was used to study the transcriptional response of S. pomeroyi cultures to additions of DMSP compared to the non-sulfur compound acetate in a time series experiment. We identified a number of upregulated genes that could be assigned to potential roles in the metabolism of DMSP. DMSP also affected the transcription of genes for transport and metabolism of peptides, amino acids and polyamines. DMSP concentration may thus also play a role as a chemical signal, indicating phytoplankton abundance and eliciting a regulatory response aimed at making maximum use of available nutrients.

show abstract

“…Succinate dehydrogenase (SDH; EC 1.3.99.1) is the sole membrane-bound enzyme of the tricarboxylic acid (TCA) cycle (reviewed by Hederstedt and Rutberg, 1981;Ackrell et al, 1992). It catalyses the oxidation of succinate to fumarate with the concomitant reduction of the ubiquinone pool of the aerobic respiratory chain.…”

Section: Introductionmentioning

confidence: 99%

Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB ) gene expression in Escherichia coli

Shen

Gunsalus

1997

Molecular Microbiology

View full text Add to dashboard Cite

SummarySuccinate dehydrogenase (sdhCDAB ) gene expression in Escherichia coli is negatively regulated by the arcA and fnr gene products during anaerobic cell growth conditions. The controlled synthesis of this sole membrane-bound enzyme of the tricarboxylic acid cycle allows optimal participation in the aerobic electron transport pathway for the generation of energy via oxidative phosphorylation reactions. To understand how ArcA participates in the anaerobic repression of sdhCDAB expression, a family of sdhC-lacZ fusions was constructed and analysed in vivo. DNase I footprint and gel shift assays using purified ArcA protein revealed the location of four distinct and independent ArcA binding sites in the sdhC promoter region. ArcA sites, designated sites 1 and 2, are centred at ¹205 bp and ¹119 bp upstream of the sdhC promoter, respectively, whereas ArcA site 3 overlaps the ¹35 and ¹10 regions of the sdhC promoter. A fourth ArcA site is centred at þ 257 bp downstream of the sdhC promoter. They are bound with differing affinity by ArcA and ArcA phosphate. The in vivo studies, in combination with the in vitro studies, indicate that ArcA site 3 is necessary and sufficient for the ArcA-dependent repression of sdhC gene expression, while the DNA region containing ArcA site 2 contributes to maximal gene expression. The DNA-containing ArcA sites 1 and 4 provide minor roles in the ArcA regulation of sdhC expression. Lastly, the Fnr-dependent control of sdhCDAB gene expression was shown to occur independently of the ArcA and to require DNA sequences near the start of sdhC transcription.

show abstract

Succinate dehydrogenase--a comparative review.

Cited by 88 publications

References 69 publications

Quantitative proteomic analysis of intracytoplasmic membrane development in Rhodobacter sphaeroides

Quantitative proteomic analysis of intracytoplasmic membrane development in Rhodobacter sphaeroides

Transcriptional response of Silicibacter pomeroyi DSS‐3 to dimethylsulfoniopropionate (DMSP)

Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB ) gene expression in Escherichia coli

Contact Info

Product

Resources

About