scholarly journals Cytosolic iron superoxide dismutase is a part of the triacylglycerol biosynthetic complex in oleaginous yeast

2003 ◽  
Vol 372 (2) ◽  
pp. 587-594 ◽  
Author(s):  
Sumana RAYCHAUDHURI ◽  
Mamatha M. REDDY ◽  
Naveen R. RAJKUMAR ◽  
Ram RAJASEKHARAN
Keyword(s):  
Superoxide Dismutase ◽  
Oleaginous Yeast ◽  
Rhodotorula Glutinis ◽  
Soluble Form ◽  
Nucleotide Sequence Analysis ◽  
Iron Superoxide Dismutase ◽  
Oxidative Damages ◽  
Cdna Nucleotide Sequence ◽  
Protein Components ◽  
First Time

A novel multienzyme complex for the biosynthesis of triacylglycerol in oleaginous yeast has been identified recently in the cytosol and characterized [Gangar, Karande and Rajasekharan (2001) J. Biol. Chem. 276, 10290–10298]. Screening the library of Rhodotorula glutinis with an oligonucleotide probe derived from the N-terminal sequence of one of the protein components in the complex (21 kDa protein) resulted in the isolation of a 0.7 kb cDNA. Nucleotide sequence analysis revealed that the isolated gene codes for superoxide dismutase (SOD). Atomic absorption spectroscopy and inhibition assays showed that this cytosolic SOD utilizes Fe as its cofactor. Enzymic assays, immunoprecipitation and cross-linking experiments revealed that SOD is a part of the triacylglycerol biosynthetic complex, which could protect the substrate and the complex from oxidative damages. These results indicate for the first time the presence of iron-containing SOD in a soluble form in yeast.

Effect of Hubs in Amino Acid Network on Iron Superoxide Dismutase Stability

2015 ◽  
Vol 10 (2) ◽  
pp. 232-239
Author(s):  
Yanrui Ding ◽  
Xueqin Wang ◽  
Zhaolin Mou
Keyword(s):  
Superoxide Dismutase ◽  
Amino Acid ◽  
Iron Superoxide Dismutase

The iron content of iron superoxide dismutase: determination by anomalous scattering

1983 ◽  
Vol 218 (1210) ◽  
pp. 119-126 ◽  
Keyword(s):  
Superoxide Dismutase ◽  
Iron Content ◽  
Three Dimensional ◽  
Anomalous Scattering ◽  
Total Iron Content ◽  
Iron Site ◽  
Iron Superoxide Dismutase ◽  
Density Map ◽  
The Difference ◽  
Electron Density Map

The number of iron atoms in the dimeric iron-containing superoxide dismutase from Pseudomonas ovalis and their atomic positions have been determined directly from anomalous scattering measurements on crystals of the native enzyme. To resolve the long-standing question of the total amount of iron per molecule for this class of dismutase, the occupancy of each site was refined against the measured Bijvoet differences. The enzyme is a symmetrical dimer with one iron site in each subunit. The iron position is 9 ņ from the intersubunit interface. The total iron content of the dimer is 1.2±0.2 moles per mole of protein. This is divided between the subunits in the ratio 0.65:0.55; the difference between them is probably not significant. Since each subunit contains, on average, slightly more than half an iron atom we conclude that the normal state of this enzyme is two iron atoms per dimer but that some of the metal is lost during purification of the protein. Although the crystals are obviously a mixture of holo- and apo-enzymes, the 2.9 Å electron density map is uniformly clean, even at the iron site. We conclude that the three-dimensional structures of the iron-bound enzyme and the apoenzyme are identical.

scholarly journals A tetrameric iron superoxide dismutase from the eucaryote Tetrahymena pyriformis.

1990 ◽  
Vol 265 (29) ◽  
pp. 17680-17687
Author(s):  
D Barra ◽  
M E Schininà ◽  
F Bossa ◽  
K Puget ◽  
P Durosay ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Tetrahymena Pyriformis ◽  
Iron Superoxide Dismutase

scholarly journals Milk Protein Fragments Induce the Biosynthesis of Macedocin, the Lantibiotic Produced by Streptococcus macedonicus ACA-DC 198

2009 ◽  
Vol 76 (4) ◽  
pp. 1143-1151 ◽  
Author(s):  
Marina Georgalaki ◽  
Marina Papadelli ◽  
Elina Chassioti ◽  
Rania Anastasiou ◽  
Anastassios Aktypis ◽  
...  
Keyword(s):  
Milk Protein ◽  
Mass Spectrometric ◽  
Partial Purification ◽  
Protein Fragments ◽  
Reverse Transcription Pcr ◽  
Heat Stable ◽  
Heat Stable Protein ◽  
Tandem Mass Spectrometric ◽  
Protein Components ◽  
First Time

ABSTRACT The aim of the present work was to study the mode of the induction of the biosynthesis of macedocin, the lantibiotic produced by Streptococcus macedonicus ACA-DC 198. Macedocin was produced when the strain was grown in milk but not in MRS or M17 broth. No autoinduction mechanism was observed. Production did not depend on the presence of lactose or galactose in the culture medium or on a coculture of the producer strain with macedocin-sensitive or macedocin-resistant strains. Induction seemed to depend on the presence of one or more heat-stable protein components produced when S. macedonicus ACA-DC 198 was grown in milk. The partial purification of the induction factor was performed by a combination of chromatography methods, and its activity was confirmed by a reverse transcription-PCR approach (RT-PCR). Mass spectrometric (MS) and tandem mass spectrometric (MS/MS) analyses of an induction-active fraction showed the presence of several peptides of low molecular mass corresponding to fragments of αS1- and β-casein as well as β-lactoglobulin. The chemically synthesized αS1-casein fragment 37-55 (2,253.65 Da) was proven to be able to induce macedocin biosynthesis. This is the first time that milk protein degradation fragments are reported to exhibit a bacteriocin induction activity.

Iron-superoxide dismutase and monodehydroascorbate reductase transcripts accumulate in response to internode rubbing in tomato

2004 ◽  
Vol 327 (7) ◽  
pp. 679-686 ◽  
Author(s):  
Ichrak Ben Rejeb ◽  
Catherine Lenne ◽  
Nathalie Leblanc ◽  
Jean-Louis Julien ◽  
Saı̈da Ammar ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Monodehydroascorbate Reductase ◽  
Iron Superoxide Dismutase

scholarly journals Biodiesel generation from oleaginous yeast Rhodotorula glutinis with xylose assimilating capacity

2007 ◽  
Vol 6 (18) ◽  
pp. 2130-2134 ◽  
Author(s):  
Dai Chuan chao ◽  
Tao Jie ◽  
Xie Feng ◽  
Dai Yi jun ◽  
Zhao Mo
Keyword(s):  
Oleaginous Yeast ◽  
Rhodotorula Glutinis

scholarly journals When good ligands go bad

2014 ◽  
Vol 70 (a1) ◽  
pp. C1269-C1269
Author(s):  
Ethan Merritt
Keyword(s):  
Task Force ◽  
Structure Refinement ◽  
Binding Pocket ◽  
Software Packages ◽  
Protein Model ◽  
Protein Components ◽  
First Time ◽  
Standard Software ◽  
New Protein

"Tools for validating structural models of proteins are relatively mature and widely implemented. New protein crystallographers are introduced early on to the importance of monitoring conformance with expected φ/ψ values, favored rotamers, and local stereochemistry. The protein model is validated by the PDB at the time of deposition using criteria that are also available in the standard software packages used to refine the model being deposited. By contrast, crystallographers are typically much less familiar with procedures to validate key non-protein components of the model – cofactors, substrates, inhibitors, etc. It has been estimated that as many as a third of all ligands in the PDB exhibit preventable errors of some sort, ranging from minor deviations in expected bond angles to wholly implausible placement in the binding pocket. Following recommendations from the wwPDB Validation Task Force, the PDB recently began validating ligand geometry as an integral part of deposition processing. This means that many crystallographers will soon receive for the first time a ""grade"" on the quality of ligands in the structure they have just deposited. Some will be surprised, as I was following my first PDB deposition of 2014, at how easily bad ligand geometry can slip through the cracks in supposedly robust structure refinement protocols that their lab has used for many years. I will illustrate use of current tools for generating ligand restraints to guide model refinement. One is the jligand+coot+cprodrg pipeline integrated into the CCP4 suite. Another is the Grade web server provided as a community resource by Global Phasing Ltd. Furthermore I will show examples from recent in-house refinements of how things can still go wrong even if you do use these tools, and how we recovered. The new PDB deposition checks may expose errors in your ligand descriptions after the fact. This presentation may help you avoid introducing those errors in the first place."

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