The role of membrane bound tetraheme CymA in the anaerobic respiration of Shewanella oneidensis MR-1

2002 ◽  
Vol 30 (3) ◽  
pp. A53-A53
Author(s):  
C. Schwalb ◽  
S. K. Chapman ◽  
G. A. Reid
Keyword(s):  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Membrane Bound

scholarly journals Involvement of a Membrane-Bound Class III Adenylate Cyclase in Regulation of Anaerobic Respiration in Shewanella oneidensis MR-1

2009 ◽  
Vol 191 (13) ◽  
pp. 4298-4306 ◽  
Author(s):  
M. A. Charania ◽  
K. L. Brockman ◽  
Y. Zhang ◽  
A. Banerjee ◽  
G. E. Pinchuk ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Receptor Protein ◽  
Plasmid Replication ◽  
Chromosomal Deletion ◽  
Class Iii ◽  
Membrane Bound ◽  
Flagellum Biosynthesis ◽  
Class Iv

ABSTRACT Unlike other bacteria that use FNR to regulate anaerobic respiration, Shewanella oneidensis MR-1 uses the cyclic AMP receptor protein (CRP) for this purpose. Three putative genes, cyaA, cyaB, and cyaC, predicted to encode class I, class IV, and class III adenylate cyclases, respectively, have been identified in the genome sequence of this bacterium. Functional validation through complementation of an Escherichia coli cya mutant confirmed that these genes encode proteins with adenylate cyclase activities. Chromosomal deletion of either cyaA or cyaB did not affect anaerobic respiration with fumarate, dimethyl sulfoxide (DMSO), or Fe(III), whereas deletion of cyaC caused deficiencies in respiration with DMSO and Fe(III) and, to a lesser extent, with fumarate. A phenotype similar to that of a crp mutant, which lacks the ability to grow anaerobically with DMSO, fumarate, and Fe(III), was obtained when both cyaA and cyaC were deleted. Microarray analysis of gene expression in the crp and cyaC mutants revealed the involvement of both genes in the regulation of key respiratory pathways, such as DMSO, fumarate, and Fe(III) reduction. Additionally, several genes associated with plasmid replication, flagellum biosynthesis, and electron transport were differentially expressed in the cyaC mutant but not in the crp mutant. Our results indicated that CyaC plays a major role in regulating anaerobic respiration and may contribute to additional signaling pathways independent of CRP.

The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella

2002 ◽  
Vol 30 (4) ◽  
pp. 658-662 ◽  
Author(s):  
C. Schwalb ◽  
S. K. Chapman ◽  
G. A. Reid
Keyword(s):  
Electron Transfer ◽  
Outer Membrane ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Fumarate Reductase ◽  
Sulphur Compounds ◽  
Sequence Alignments ◽  
Membrane Bound ◽  
Periplasmic Domain

Shewanella spp. demonstrate great variability in the use of terminal electron acceptors in anaerobic respiration; these include nitrate, fumarate, DMSO, trimethylamine oxide, sulphur compounds and metal oxides. These pathways open up possible applications in bioremediation. The wide variety of respiratory substrates for Shewanella is correlated with the evolution of several multi-haem membrane-bound, periplasmic and outer-membrane c-type cytochromes. The 21 kDa c-type cytochrome CymA of the freshwater strain Shewanella oneidensis MR-1 has an N-terminal membrane anchor and a globular tetrahaem periplasmic domain. According to sequence alignments, CymA is a member of the NapC/NirT family. This family of redox proteins is responsible for electron transfer from the quinone pool to periplasmic and outer-membrane-bound reductases. Prior investigations have shown that the absence of CymA results in loss of the ability to respire with Fe(III), fumarate and nitrate, indicating that CymA is involved in electron transfer to several terminal reductases. Here we describe the expression, purification and characterization of a soluble, truncated CymA (‘CymA). Potentiometric studies suggest that there are two pairs of haems with potentials of -175 and -261 mV and that ‘CymA is an efficient electron donor for the soluble fumarate reductase, flavocytochrome c3.

scholarly journals Respiration and Growth of Shewanella oneidensis MR-1 Using Vanadate as the Sole Electron Acceptor

2005 ◽  
Vol 187 (10) ◽  
pp. 3293-3301 ◽  
Author(s):  
Wesley Carpentier ◽  
Lina De Smet ◽  
Jozef Van Beeumen ◽  
Ann Brigé
Keyword(s):  
Electron Acceptor ◽  
Manganese Oxides ◽  
Proton Translocation ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Difference Spectra ◽  
Free Living ◽  
E Coli ◽  
Membrane Bound ◽  
Iron And Manganese

ABSTRACT Shewanella oneidensis MR-1 is a free-living gram-negative γ-proteobacterium that is able to use a large number of oxidizing molecules, including fumarate, nitrate, dimethyl sulfoxide, trimethylamine N-oxide, nitrite, and insoluble iron and manganese oxides, to drive anaerobic respiration. Here we show that S. oneidensis MR-1 is able to grow on vanadate as the sole electron acceptor. Oxidant pulse experiments demonstrated that proton translocation across the cytoplasmic membrane occurs during vanadate reduction. Proton translocation is abolished in the presence of protonophores and the inhibitors 2-heptyl-4-hydroxyquinoline N-oxide and antimycin A. Redox difference spectra indicated the involvement of membrane-bound menaquinone and cytochromes c, which was confirmed by transposon mutagenesis and screening for a vanadate reduction-deficient phenotype. Two mutants which are deficient in menaquinone synthesis were isolated. Another mutant with disruption in the cytochrome c maturation gene ccmA was unable to produce any cytochrome c and to grow on vanadate. This phenotype could be restored by complementation with the pEC86 plasmid expressing ccm genes from Escherichia coli. To our knowledge, this is the first report of E. coli ccm genes being functional in another organism. Analysis of an mtrB-deficient mutant confirmed the results of a previous paper indicating that OmcB may function as a vanadate reductase or may be part of a vanadate reductase complex.

scholarly journals Periplasmic Electron Transfer via the c-Type Cytochromes MtrA and FccA of Shewanella oneidensis MR-1

2009 ◽  
Vol 75 (24) ◽  
pp. 7789-7796 ◽  
Author(s):  
Bjoern Schuetz ◽  
Marcus Schicklberger ◽  
Johannes Kuermann ◽  
Alfred M. Spormann ◽  
Johannes Gescher
Keyword(s):  
Electron Transfer ◽  
Cytoplasmic Membrane ◽  
Shewanella Oneidensis ◽  
Microbial Reduction ◽  
Fumarate Reductase ◽  
Mineral Phase ◽  
Membrane Bound ◽  
Growth Experiments

ABSTRACT Dissimilatory microbial reduction of insoluble Fe(III) oxides is a geochemically and ecologically important process which involves the transfer of cellular, respiratory electrons from the cytoplasmic membrane to insoluble, extracellular, mineral-phase electron acceptors. In this paper evidence is provided for the function of the periplasmic fumarate reductase FccA and the decaheme c-type cytochrome MtrA in periplasmic electron transfer reactions in the gammaproteobacterium Shewanella oneidensis. Both proteins are abundant in the periplasm of ferric citrate-reducing S. oneidensis cells. In vitro fumarate reductase FccA and c-type cytochrome MtrA were reduced by the cytoplasmic membrane-bound protein CymA. Electron transfer between CymA and MtrA was 1.4-fold faster than the CymA-catalyzed reduction of FccA. Further experiments showing a bidirectional electron transfer between FccA and MtrA provided evidence for an electron transfer network in the periplasmic space of S. oneidensis. Hence, FccA could function in both the electron transport to fumarate and via MtrA to mineral-phase Fe(III). Growth experiments with a ΔfccA deletion mutant suggest a role of FccA as a transient electron storage protein.

A ROLE OF PROTEINS OF THE OUTER MEMBRANE OF Shewanella oneidensis MR-1 BACTERIA IN FORMATION AND STABILIZATION OF SILVER SULFIDE NANOPARTICLES

2015 ◽  
pp. 41-48 ◽  
Author(s):  
T. A. Voeikova ◽  
A. S. Shebanova ◽  
Yu. D. Ivanov ◽  
A. L. Kaysheva ◽  
L. M. Novikova ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Shewanella Oneidensis ◽  
Silver Sulfide ◽  
Silver Sulfide Nanoparticles

Anaerobic Respiration on Nitarsone in Aquatic Environments by Shewanella oneidensis MR-1 Lacking Known C·As lyases

2020 ◽  
Author(s):  
Dong-Feng Liu ◽  
Xue-Na Huang ◽  
Rui-Fen Cheng ◽  
Di Min ◽  
Lei Cheng ◽  
...  
Keyword(s):  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Aquatic Environments

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 Advances in understanding the role of cardiac glycosides in control of sodium transport in renal tubules

2014 ◽  
Vol 222 (1) ◽  
pp. R11-R24 ◽  
Author(s):  
Syed Jalal Khundmiri
Keyword(s):  
Heart Failure ◽  
Intracellular Signaling ◽  
Cardiac Contractility ◽  
Myocardial Cell ◽  
Renal Tubules ◽  
Intracellular Signaling Pathway ◽  
Body Sodium ◽  
Membrane Bound ◽  
Total Body

Cardiotonic steroids have been used for the past 200 years in the treatment of congestive heart failure. As specific inhibitors of membrane-bound Na+/K+ATPase, they enhance cardiac contractility through increasing myocardial cell calcium concentration in response to the resulting increase in intracellular Na concentration. The half-minimal concentrations of cardiotonic steroids required to inhibit Na+/K+ATPase range from nanomolar to micromolar concentrations. In contrast, the circulating levels of cardiotonic steroids under physiological conditions are in the low picomolar concentration range in healthy subjects, increasing to high picomolar levels under pathophysiological conditions including chronic kidney disease and heart failure. Little is known about the physiological function of low picomolar concentrations of cardiotonic steroids. Recent studies have indicated that physiological concentrations of cardiotonic steroids acutely stimulate the activity of Na+/K+ATPase and activate an intracellular signaling pathway that regulates a variety of intracellular functions including cell growth and hypertrophy. The effects of circulating cardiotonic steroids on renal salt handling and total body sodium homeostasis are unknown. This review will focus on the role of low picomolar concentrations of cardiotonic steroids in renal Na+/K+ATPase activity, cell signaling, and blood pressure regulation.

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