Unique Isozymes of Superoxide Dismutase inStreptomyces griseus

Youn, Hong Duk; Youn, Hwan; Lee, Jinwon; Yim, Yang In; Lee, Jeong Kug; Hah, Yung Chil; Kang, Shinjae

doi:10.1006/abbi.1996.0463

Cited by 134 publications

(93 citation statements)

References 3 publications

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“…The evidence for a Ni ion in the active site came first from EPR spectra (7). A subsequent 61 Ni isotope substitution experiment (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…All clinical and soil isolates of Streptomyces reported to date possess this cytoplasmic NiSOD, and for some strains the additional presence of an Fe(Zn)SOD was reported (7,10,11). NiSOD is distinct from the Mn-, Fe-, or Cu,ZnSODs on the basis of amino acid sequence, immunological crossreactivity, and spectroscopic properties.…”

mentioning

confidence: 99%

“…Recently, a SOD with only nickel in the active site (NiSOD) was purified from several aerobic soil bacteria of the Streptomyces species (7)(8)(9). All clinical and soil isolates of Streptomyces reported to date possess this cytoplasmic NiSOD, and for some strains the additional presence of an Fe(Zn)SOD was reported (7,10,11).…”

mentioning

confidence: 99%

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Crystal structure of nickel-containing superoxide dismutase reveals another type of active site

Wuerges

Lee

Yim

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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325

403

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Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.

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“…The evidence for a Ni ion in the active site came first from EPR spectra (7). A subsequent 61 Ni isotope substitution experiment (Fig.…”

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Crystal structure of nickel-containing superoxide dismutase reveals another type of active site

Wuerges

Lee

Yim

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

325

403

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“…SodF converts the superoxide anion to hydrogen peroxide and molecular oxygen, catalyzed by cyclic oxidation and reduction of the transition metal in the active site of superoxide dismutases (31). SodF was identified as a cytoplasmic protein in S. griseus (32) and as an extracellular enzyme in S. pristinaespiralis (30). Because the intracellular and extracellular isoforms have the same molecular weight, SodF may well be autotransported as a leaderless protein (33).…”

Section: Resultsmentioning

confidence: 99%

The Secreted Signaling Protein Factor C Triggers the A-factor Response Regulon in Streptomyces griseus

Birkó

Bialek

Buzás

et al. 2007

Molecular & Cellular Proteomics

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Members of the prokaryotic genus Streptomyces produce over 60% of all known antibiotics and a wide range of industrial enzymes. A leading theme in microbiology is which signals are received and transmitted by these organisms to trigger the onset of morphological differentiation and antibiotic production. The small ␥-butyrolactone A-factor is an important autoregulatory signaling molecule in streptomycetes, and A-factor mutants are blocked in development and antibiotic production. In this study we showed that heterologous expression of the 324-amino acid secreted regulatory protein Factor C resulted in restoration of development and enhanced antibiotic production of an A-factor-deficient bald mutant of Streptomyces griseus, although the parental strain lacks an facC gene. Proteome analysis showed that in the facC transformant the production of several secreted proteins that belong to the A-factor regulon was restored. HPLC-MS/MS analysis indicated that this was due to restoration of A-factor production to wild-type levels in the transformant. This indicates a connection between two highly divergent types of signaling molecules and possible interplay between their regulatory networks.

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“…The prokaryotic MnSOD, FeSOD and eukaryotic Cu/ZnSOD are dimers, whereas MnSOD of mitochondria are tetramers. NiSOD is the most recent class of SOD, which was discovered in Streptomyces [205] and cyanobacteria [144]. On the basis of amino acid sequence, metal ligand environment, and spectroscopic properties, NiSOD is distinct from other known SODs [28,87].…”

Section: Superoxide Dismutase (Sod)mentioning

confidence: 99%