Purification and Some Properties of Cytochrome c-552 from an Extreme Thermophile, Thermus thermophilus HB81

Hon-Nami, Koyu; Oshima, Tairo

doi:10.1093/oxfordjournals.jbchem.a131753

Cited by 64 publications

(45 citation statements)

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“…A signal having the parameters re- ported for horse heart cytochrome c (29) has not been observed. The relationship of this c type cytochrome, which has its a band at 550 nm, to the solubilized c cytochromes c-552 and c-554 isolated from T. thermophilus by Hon-Nami and Oshima (30,31) is not known.…”

Section: Resultsmentioning

confidence: 98%

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Fee¹,

Choc²,

Findling³

et al. 1980

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

102

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Section: Resultsmentioning

confidence: 98%

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Fee¹,

Choc²,

Findling³

et al. 1980

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

102

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“…The optical purity ratio A 408 0A 280 of our best preparations is 4.7 compared to 4. 7~Hon-nami &Oshima, 1977! and5.1~Yoshida et al, 1984! reported previously for the native protein, and gel electrophoresis revealed a single band~data not shown!.…”

Section: Biochemical Observationsmentioning

confidence: 99%

Integrity of thermus thermophilus cytochrome c₅₅₂ Synthesized by escherichia coli cells expressing the host‐specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein

et al. 2000

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We describe the design of Escherichia coli cells that synthesize a structurally perfect, recombinant cytochrome c from the Thermus thermophilus cytochrome c 552 gene. Key features are~1! construction of a plasmid-borne, chimeric cycA gene encoding an Escherichia coli-compatible, N-terminal signal sequence~MetLysIleSerIleTyrAlaThrLeu AlaAlaLeuSerLeuAlaLeuProAlaGlyAla! followed by the amino acid sequence of mature Thermus cytochrome c 552 ; and~2! coexpression of the chimeric cycA gene with plasmid-borne, host-specific cytochrome c maturation genes ccmABCDEFGH !. Approximately 1 mg of purified protein is obtained from 1 L of culture medium. The recombinant protein, cytochrome rsC 552 , and native cytochrome c 552 have identical redox potentials and are equally active as electron transfer substrates toward cytochrome ba 3 , a Thermus heme-copper oxidase. Native and recombinant cytochromes c were compared and found to be identical using circular dichroism, optical absorption, resonance Raman, and 500 MHz 1 H-NMR spectroscopies. The 1.7 Å resolution X-ray crystallographic structure of the recombinant protein was determined and is indistinguishable from that reported for the native protein~Than, ME, Hof P, Huber R, Bourenkov GP, Bartunik HD, Buse G, Soulimane T, 1997, J Mol Biol 271:629-644!. This approach may be generally useful for expression of alien cytochrome c genes in E. coli. Keywords: cytochrome c; Escherichia coli; homologous expression; Thermus thermophilusAlthough studied for many decades as part of the cell's respiratory apparatus~Lemberg & Barrett, 1973;Mathews, 1985;Pettigrew & Moore, 1987!, cytochromes c remain of considerable interest as objects in the study of electron transfer reactions~Ferguson-Miller et al., 1979;Pan et al., 1993;Bjerrum et al., 1995;Geren et al., 1995;Winkler et al., 1995! and of protein folding~Sosnick et al., 1994;Bryngelson et al., 1995;Mines et al., 1996;Bai, 1999!. In addition, recent evidence indicates that cytochrome c released from the mitochondrion is able to initiate apoptosis~Wallace, 1999, and references therein!, suggesting that this protein may have functions other than electron transfer. Today, application of modern experimental approaches to cytochrome c function can be limited by the general unavailability of suitable expression systems for cloned cytochrome c genes. Escherichia coli is certainly the organism of choice, but most attempts to express foreign cytochrome c genes in this bacterium have been unsuccessful; either the yield is imprac-

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“…Electrons are transferred to menaquinone-8, the major quinone in the membrane of this organism (38). The corresponding quinol is oxidized by heterotetrameric complex III (39,40), which donates the electrons to the terminal oxidases (complex IV) through soluble periplasmic cytochrome c 552 (41,42). There are two terminal cytochrome oxidases in this bacterium: caa 3 , expressed under conditions of fully aerobic growth, and ba 3 , induced under low oxygen pressures (43)(44)(45)(46)(47).…”

mentioning

confidence: 99%

Transferable Denitrification Capability of Thermus thermophilus

Álvarez

Bricio

Blesa

et al. 2014

Appl Environ Microbiol

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Laboratory-adapted strains of Thermus spp. have been shown to require oxygen for growth, including the model strains T. thermophilus HB27 and HB8. In contrast, many isolates of this species that have not been intensively grown under laboratory conditions keep the capability to grow anaerobically with one or more electron acceptors. The use of nitrogen oxides, especially nitrate, as electron acceptors is one of the most widespread capabilities among these facultative strains. In this process, nitrate is reduced to nitrite by a reductase (Nar) that also functions as electron transporter toward nitrite and nitric oxide reductases when nitrate is scarce, effectively replacing respiratory complex III. In many T. thermophilus denitrificant strains, most electrons for Nar are provided by a new class of NADH dehydrogenase (Nrc). The ability to reduce nitrite to NO and subsequently to N 2 O by the corresponding Nir and Nor reductases is also strain specific. The genes encoding the capabilities for nitrate (nar) and nitrite (nir and nor) respiration are easily transferred between T. thermophilus strains by natural competence or by a conjugation-like process and may be easily lost upon continuous growth under aerobic conditions. The reason for this instability is apparently related to the fact that these metabolic capabilities are encoded in gene cluster islands, which are delimited by insertion sequences and integrated within highly variable regions of easily transferable extrachromosomal elements. Together with the chromosomal genes, these plasmid-associated genetic islands constitute the extended pangenome of T. thermophilus that provides this species with an enhanced capability to adapt to changing environments.

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Purification and Some Properties of Cytochrome c-552 from an Extreme Thermophile, Thermus thermophilus HB81

Cited by 64 publications

References 0 publications

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Integrity of thermus thermophilus cytochrome c₅₅₂ Synthesized by escherichia coli cells expressing the host‐specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein

Transferable Denitrification Capability of Thermus thermophilus

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Purification and Some Properties of Cytochrome c-552 from an Extreme Thermophile, Thermus thermophilus HB81

Cited by 64 publications

References 0 publications

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Integrity of thermus thermophilus cytochrome c552 Synthesized by escherichia coli cells expressing the host‐specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein

Transferable Denitrification Capability of Thermus thermophilus

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Integrity of thermus thermophilus cytochrome c₅₅₂ Synthesized by escherichia coli cells expressing the host‐specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein