A Bacterial Cytochrome c Heme Lyase

Ren, Qun; Ahuja, Umesh; Thöny‐Meyer, Linda

doi:10.1074/jbc.m110979200

Cited by 94 publications

(75 citation statements)

References 25 publications

(21 reference statements)

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“…The detection of both proteins in various complexes argues in favor of transient interactions between CCM proteins. We propose that the complex containing both CCMH and CcmF N2 in plants could hold the heme lyase activity, as already suggested by other experiments in bacteria (13).…”

Section: Discussionsupporting

confidence: 57%

“…In E. coli, neither successful coimmunoprecipitation nor detection of mixed disulfides between CcmH and apocytochromes has been reported (13). Similarly, AtCCMH and apocytochrome c coimmunoprecipitation was unsuccessful in our hands.…”

Section: Discussionmentioning

confidence: 38%

“…For coimmunoprecipitation experiments, 500 g of E. coli membrane proteins were solubilized and precipitated with 5 l of anti-CcmF antibodies (13) according to previous work (12). E. coli spheroplasts were prepared by treatment with 8 g͞ml lysozyme in 100 mM Tris⅐HCl (pH 8.0) containing 20% sucrose.…”

Section: Coexpression Of Atccmh and Ecccm Proteinsmentioning

confidence: 99%

“…CcmC is required for the covalent attachment of heme to the heme chaperone CcmE (10)(11)(12). CcmF has been proposed to form a bacterial cytochrome c heme lyase complex together with CcmH (13). Cysteine thiols of the heme-binding motif of apocytochromes c are oxidized by the periplasmic DsbA.…”

mentioning

confidence: 99%

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AtCCMH, an essential component of thec-type cytochrome maturation pathway inArabidopsismitochondria, interacts with apocytochromec

Meyer

Giegé

Gelhaye

et al. 2005

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

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The maturation of c-type cytochromes requires the covalent ligation of the heme cofactor to reduced cysteines of the CXXCH motif of apocytochromes. In contrast to mitochondria of other eukaryotes, plant mitochondria follow a pathway close to that found in ␣-and ␥-proteobacteria. We identified a nuclear-encoded protein, AtCCMH, the Arabidopsis thaliana ortholog of bacterial CcmH͞CycL proteins. In bacteria, CcmH and the thioredoxin CcmG are components of a periplasmic thio-reduction pathway proposed to maintain the apocytochrome c cysteines in a reduced state. AtCCMH is located exclusively in mitochondria. AtCCMH is an integral protein of the inner membrane with the conserved RCXXC motif facing the intermembrane space. Reduction assays show that the cysteine thiols in the RCXXC motif of AtCCMH can form a disulfide bond that can be reduced by enzymatic thiol reductants.

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Section: Discussionsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 38%

Section: Coexpression Of Atccmh and Ecccm Proteinsmentioning

confidence: 99%

mentioning

confidence: 99%

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AtCCMH, an essential component of thec-type cytochrome maturation pathway inArabidopsismitochondria, interacts with apocytochromec

Meyer

Giegé

Gelhaye

et al. 2005

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

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“…1A) comprises the membrane-bound proteins CcmABCDEFGH. CcmA, CcmB, and CcmC form an ABC-type transporter, the function of which is unknown (20,21), although it is known that CcmC, together with CcmE, is involved in heme delivery to the cytochrome c heme lyase complex consisting of CcmFH (22)(23)(24)(25)(26). Reduction of the cysteinyls of the Cys-Xxx-Xxx-Cys-His motif prior to heme insertion is accomplished by CcmG and CcmH, but it is not clear whether the electrons flow from CcmG by means of CcmH, or from CcmH via CcmG, to the apo-cytochrome (27,28).…”

mentioning

confidence: 99%

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Crow

Acheson

Brun

et al. 2004

Journal of Biological Chemistry

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Post-translational maturation of cytochromes c involves the covalent attachment of heme to the Cys-XxxXxx-Cys-His motif of the apo-cytochrome. For this process, the two cysteines of the motif must be in the reduced state. In bacteria, this is achieved by dedicated, membrane-bound thiol-disulfide oxidoreductases with a high reducing power, which are essential components of cytochrome c maturation systems and are also linked to cellular disulfide-bond formation machineries. Here we report high-resolution structures of oxidized and reduced states of a soluble, functional domain of one such oxidoreductase, ResA, from Bacillus subtilis. The structures elucidate the structural basis of the protein's high reducing power and reveal the largest redox-coupled conformational changes observed to date in any thioredoxin-like protein. These redox-coupled changes alter the protein surface and illustrate how the redox state of ResA predetermines to which substrate it binds. Furthermore, a polar cavity, present only in the reduced state, may confer specificity to recognize apo-cytochrome c. The described features of ResA are likely to be general for bacterial cytochrome c maturation systems.

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Thermal properties of poly(vinyl alcohol)/poly(diallyldi‐methylammonium chloride) interpenetrating polymer networks

Kim

Yoon

Lee

et al. 2003

J of Applied Polymer Sci

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ABSTRACT:Interpenetrating polymer networks (IPNs) constructed with poly(vinyl alcohol) (PVA) and poly(diallyldimethyl ammonium chloride) (PDADMAC) using a sequential IPN method were prepared. The thermal characterization of the IPNs was investigated by differential scanning calorimetry (DSC), dielectric analysis (DEA), and thermogravimtric analysis (TGA). Decreases in the melting temperature of PVA segments in IPNs were observed with increasing PDADMAC content using DSC. DEA was employed to ascertain glass transition temperature of IPNs. The thermal decomposition of IPNs was investigated using TGA, and thermal decomposition of IPNs could be decelerated by changing PVA content.

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A Bacterial Cytochrome c Heme Lyase

Cited by 94 publications

References 25 publications

AtCCMH, an essential component of thec-type cytochrome maturation pathway inArabidopsismitochondria, interacts with apocytochromec

AtCCMH, an essential component of thec-type cytochrome maturation pathway inArabidopsismitochondria, interacts with apocytochromec

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Thermal properties of poly(vinyl alcohol)/poly(diallyldi‐methylammonium chloride) interpenetrating polymer networks

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