scholarly journals The roles of CymA in support of the respiratory flexibility of Shewanella oneidensis MR-1

2012 ◽  
Vol 40 (6) ◽  
pp. 1217-1221 ◽  
Author(s):  
Sophie J. Marritt ◽  
Duncan G.G. McMillan ◽  
Liang Shi ◽  
James K. Fredrickson ◽  
John M. Zachara ◽  
...  
Keyword(s):  
Shewanella Oneidensis ◽  
Model Organism ◽  
Anaerobic Growth ◽  
Biochemical Basis ◽  
Shewanella Species ◽  
Respiratory Chains ◽  
Space Colonization ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic ◽  
Respiratory Electron Transport

Shewanella species are isolated from the oxic/anoxic regions of seawater and aquatic sediments where redox conditions fluctuate in time and space. Colonization of these environments is by virtue of flexible respiratory chains, many of which are notable for the ability to reduce extracellular substrates including the Fe(III) and Mn(IV) contained in oxide and phyllosilicate minerals. Shewanella oneidensis MR-1 serves as a model organism to consider the biochemical basis of this flexibility. In the present paper, we summarize the various systems that serve to branch the respiratory chain of S. oneidensis MR-1 in order that electrons from quinol oxidation can be delivered the various terminal electron acceptors able to support aerobic and anaerobic growth. This serves to highlight several unanswered questions relating to the regulation of respiratory electron transport in Shewanella and the central role(s) of the tetrahaem-containing quinol dehydrogenase CymA in that process.

scholarly journals Constitutive Expression of Escherichia coli tat Genes Indicates an Important Role for the Twin-Arginine Translocase during Aerobic and Anaerobic Growth

2001 ◽  
Vol 183 (5) ◽  
pp. 1801-1804 ◽  
Author(s):  
Rachael L. Jack ◽  
Frank Sargent ◽  
Ben C. Berks ◽  
Gary Sawers ◽  
Tracy Palmer
Keyword(s):  
Constitutive Expression ◽  
Protein Export ◽  
The Other ◽  
Anaerobic Growth ◽  
Transcription Start ◽  
Transcription Start Sites ◽  
Expression Studies ◽  
Twin Arginine Translocase ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

ABSTRACT The transcription start sites for the tatABCD andtatE loci, encoding components of the Tat (twin-arginine translocase) protein export pathway, have been identified. Expression studies indicate that the tatABCD and tatEtranscription units are expressed constitutively. Translational fusion experiments suggest that TatA is synthesized at a much higher level than the other Tat proteins.

Metabolic and transcriptomic profiling of Streptococcus intermedius during aerobic and anaerobic growth

Metabolomics ◽  
2016 ◽  
Vol 12 (3) ◽  
Author(s):  
Fan Fei ◽  
Michelle L. Mendonca ◽  
Brian E. McCarry ◽  
Dawn M. E. Bowdish ◽  
Michael G. Surette
Keyword(s):  
Anaerobic Growth ◽  
Streptococcus Intermedius ◽  
Transcriptomic Profiling ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

scholarly journals Growth and Amino Acid Requirements of Various Strains of Group B Streptococci

1978 ◽  
Vol 7 (1) ◽  
pp. 28-33
Author(s):  
Thomas W. Milligan ◽  
Terence I. Doran ◽  
David C. Straus ◽  
Stephen J. Mattingly
Keyword(s):  
Amino Acid ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Clinical Isolates ◽  
Group B Streptococci ◽  
Amino Acid Requirements ◽  
Group B ◽  
Doubling Times ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

A chemically defined medium (FMC; B. Terleckyj, N. P. Willett, and G. D. Shockman, Infect. Immun. 11 :649-655, 1975) was used to compare the growth and amino acid requirements of 16 strains of group B streptococci, consisting of both laboratory-passaged organisms and fresh clinical isolates from adult and neonatal infections. The 5 standard Lancefield immunizing strains of group B streptococci, 090 (Ia), H36B (Ib), A909 (Ic), 18RS21 (II), and D136C (III), had doubling times in FMC (28 to 36 min) similar to those observed in Todd-Hewitt glucose broth (24 to 30 min). Similar doubling times were obtained with 11 clinical isolates growing in Todd-Hewitt glucose broth and FMC. The optimum buffering capacity of FMC was provided by 0.06 M sodium phosphate, and 1% glucose gave maximum cell yield. The group B streptococci, with minor exceptions, were very homogeneous in their amino acid requirements under both aerobic and anaerobic growth conditions. Phenylalanine, tyrosine, tryptophan, glutamate, arginine, valine, leucine, lysine, methionine, isoleucine, cystine, and histidine were required by all 16 strains under both aerobic and anaerobic growth conditions. In addition, threonine was required by all strains under aerobic growth conditions, whereas only 9 strains required threonine under anaerobic conditions. Serine was required by only 3 type III fresh clinical isolates aerobically, but not anaerobically. A requirement for glycine varied from strain to strain, apparently influenced by the oxidation-reduction potential of the growth medium.

scholarly journals Staphylococcus aureusCoproporphyrinogen III Oxidase Is Required for Aerobic and Anaerobic Heme Synthesis

mSphere ◽  
2019 ◽  
Vol 4 (4) ◽  
Author(s):  
Jacob E. Choby ◽  
Eric P. Skaar
Keyword(s):  
Staphylococcus Aureus ◽  
Anaerobic Respiration ◽  
Model Organism ◽  
Anaerobic Growth ◽  
Cellular Respiration ◽  
Nitrate Respiration ◽  
Human Pathogen ◽  
Content Type ◽  
Heme Synthesis ◽  
Aerobic And Anaerobic

ABSTRACTThe virulence of the human pathogenStaphylococcus aureusis supported by many heme-dependent proteins, including key enzymes of cellular respiration. Therefore, synthesis of heme is a critical component of staphylococcal physiology.S. aureusgenerates heme via the coproporphyrin-dependent pathway, conserved across members of theFirmicutesandActinobacteria. In this work, we genetically investigate the oxidation of coproporphyrinogen to coproporphyrin in this heme synthesis pathway. The coproporphyrinogen III oxidase CgoX has previously been identified as the oxygen-dependent enzyme responsible for this conversion under aerobic conditions. However, becauseS. aureususes heme during anaerobic nitrate respiration, we hypothesized that coproporphyrin production is able to proceed in the absence of oxygen. Therefore, we tested the contribution to anaerobic heme synthesis of CgoX and two other proteins previously identified as potential oxygen-independent coproporphyrinogen dehydrogenases, NWMN_1486 and NWMN_1636. We have found that CgoX alone is responsible for aerobic and anaerobic coproporphyrin synthesis from coproporphyrinogen and is required for aerobic and anaerobic heme-dependent growth. This work provides an explanation for howS. aureusheme synthesis proceeds under both aerobic and anaerobic conditions.IMPORTANCEHeme is a critical molecule required for aerobic and anaerobic respiration by organisms across kingdoms. The human pathogenStaphylococcus aureushas served as a model organism for the study of heme synthesis and heme-dependent physiology and, like many species of the phylaFirmicutesandActinobacteria, generates heme through a coproporphyrin intermediate. A critical step in terminal heme synthesis is the production of coproporphyrin by the CgoX enzyme, which was presumed to be oxygen dependent. However,S. aureusalso requires heme during anaerobic growth; therefore, the synthesis of coproporphyrin by an oxygen-independent mechanism is required. Here, we identify CgoX as the enzyme performing the oxygen-dependent and -independent synthesis of coproporphyrin from coproporphyrinogen, resolving a key outstanding question in the coproporphyrin-dependent heme synthesis pathway.

Fumarate dependent protein composition under aerobic and anaerobic growth conditions in Escherichia coli

2020 ◽  
Vol 212 ◽  
pp. 103583 ◽  
Author(s):  
Kristin Surmann ◽  
Marius Stopp ◽  
Sebastian Wörner ◽  
Vishnu M. Dhople ◽  
Uwe Völker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Composition ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Dependent Protein ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic
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