A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis; in vitro and in vivo studies

Monika, Elizabeth M.; Goldman, Barry S.; Beckman, Diana L.; Kranz, Robert G.

doi:10.1006/jmbi.1997.1227

Cited by 77 publications

(153 citation statements)

References 66 publications

Supporting

Mentioning

145

Contrasting

Order By: Relevance

“…We tested the reducing activity of AtCCMH in the insulin reduction assay (35). Similar to its bacterial homologue RcCcl2 (18), AtCCMH (in excess) was unable to reduce insulin in vitro (data not shown).…”

Section: Identification and Expression Of Atccmhmentioning

confidence: 92%

“…Bacterial CcmH proteins are inserted into the cytoplasmic membrane with their N-terminal domain localized in the periplasm (18,19). Mitochondrial subfractions were analyzed to check AtCCMH location and topology.…”

Section: Identification and Expression Of Atccmhmentioning

confidence: 99%

“…CcmH proteins possess an RCXXC motif exposed to the periplasm. This motif is believed to be active in the reduction of the cysteines of the CXXCH motif on apocytochromes c (18,19). Because in fungal and animal mitochondria system III is used for cytochromes c maturation, the occurrence of bacterial system I ccm orthologs in plant mitochondrial genomes was unexpected.…”

mentioning

confidence: 99%

See 2 more Smart Citations

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.

View full text Add to dashboard Cite

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.

show abstract

Section: Identification and Expression Of Atccmhmentioning

confidence: 92%

Section: Identification and Expression Of Atccmhmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

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.

View full text Add to dashboard Cite

show abstract

“…TRX maintains a reducing environment in the cytoplasm by reverting disulfide bonds to dithiols in cytoplasmic proteins (12). However, the redox activity of CcmG is different from that of TRX and TRX-like proteins in that it is highly specific and limited to cytochrome c maturation (10,23). Furthermore, CcmG, unlike other TRX-like proteins, is not a catalyst of the insulin reduction assay (10).…”

mentioning

confidence: 99%

The Acidic Nature of the CcmG Redox-Active Center Is Important for CytochromecMaturation inEscherichia coli

et al. 2004

View full text Add to dashboard Cite

show abstract

“…The use of thioredoxinderived reducing equivalents is a fundamental requirement for a variety of bacterial extracellular and periplasmic activities, such as the activities of the disulfide bond forming (Dsb) system, the crosslinking of spore coat proteins, and CCM. These processes cannot be controlled by concentration dependence alone; and, in the case of CCM, genetic elimination of the terminal thioredoxin-like protein has been shown to specifically abolish maturation of c-type cytochromes for a number of systems (5,14,31,32). Crow et al (21) presented a structure-based theory that ResA (system II CCM) uses redox-coupled conformational changes to select its substrate.…”

Section: Resultsmentioning

confidence: 99%

Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation

Colbert¹,

Erbel

et al. 2006

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

View full text Add to dashboard Cite

The covalent attachment of heme cofactors to the apo-polypeptides via thioether bonds is unique to the maturation of c-type cytochromes. A number of thiol-disulfide oxidoreductases prepare the apocytochrome for heme insertion in system I and II cytochrome c maturation. Although most thiol-disulfide oxidoreductases are nonspecific, the less common, specific thiol-disulfide oxidoreductases may be key to directing the usage of electrons. Here we demonstrate that unlike other thiol-disulfide oxidoreductases, the protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific for cytochrome c550 and utilizes alternate conformations to recognize redox partners. We report solution NMR evidence that ResA undergoes a redox-dependent conformational change between oxidation states, as well as data showing that ResA utilizes a surface cavity present only in the reduced state to recognize a peptide derived from cytochrome c550. Finally, we confirm that ResA is a specific thiol-disulfide oxidoreductase by comparing its reactivity to our mimetic peptide with its reactivity to oxidized glutathione, a nonspecific substrate. This study biochemically demonstrates the specificity of this thioldisulfide oxidoreductase and enables us to outline a structural mechanism of regulating the usage of electrons in a thiol-disulfide oxidoreductase system. NMR ͉ thiol-disulfide oxidoreductase ͉ x-ray crystallography

show abstract

A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis; in vitro and in vivo studies

Cited by 77 publications

References 66 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

The Acidic Nature of the CcmG Redox-Active Center Is Important for CytochromecMaturation inEscherichia coli

Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation

Contact Info

Product

Resources

About