<i>Saccharomyces cerevisiae</i> Cox18 complements the essential Sec‐independent function of <i>Escherichia coli</i> YidC

Bloois, Edwin van; Koningstein, Gregory M.; Bauerschmitt, Heike; Herrmann, Johannes M.; Luirink, Joen

doi:10.1111/j.1742-4658.2007.06094.x

Cited by 23 publications

(13 citation statements)

References 49 publications

(119 reference statements)

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“…Nevertheless, to a large extent they are functionally conserved and even appear to be generally exchangeable (18,31,45). Our results confirm this general trend, since the two YidC homologs from the gram-positive bacterium B. subtilis completely restore growth of YidC-depleted E. coli cells both on agar plates and in liquid medium.…”

Section: Discussionsupporting

confidence: 81%

Bacillus subtilis SpoIIIJ and YqjG Function in Membrane Protein Biogenesis

Saller

Driessen

2009

J Bacteriol

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Section: Discussionsupporting

confidence: 81%

Bacillus subtilis SpoIIIJ and YqjG Function in Membrane Protein Biogenesis

Saller

Driessen

2009

J Bacteriol

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“…Oxa1 members have an extra C terminus region that binds to the ribosome (20), whereas bacterial YidC proteins contain an additional N-terminal transmembrane domain required for membrane targeting (21). Several studies have tested the functional overlapping between Oxa1/YicC and Cox18 in different organisms, particularly the fungi S. cerevisiae, Schizosaccharomyces pombe, and Neurospora crassa and the bacterium Escherichia coli (18,(22)(23)(24). Mild to extremely weak heterologous complementation by overexpression of chimeric proteins has been observed among members of this family (18,(22)(23)(24).…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have tested the functional overlapping between Oxa1/YicC and Cox18 in different organisms, particularly the fungi S. cerevisiae, Schizosaccharomyces pombe, and Neurospora crassa and the bacterium Escherichia coli (18,(22)(23)(24). Mild to extremely weak heterologous complementation by overexpression of chimeric proteins has been observed among members of this family (18,(22)(23)(24). For example, YidC can partially complement an S. cerevisiae cox18 deletion strain (23), and a fusion of the extra N terminus transmembrane domain of YidC to ScCox18 or ScOxa1 can partially comple- ment the absence of YidC in E. coli (24).…”

Section: Discussionmentioning

confidence: 99%

Human mitochondrial cytochrome c oxidase assembly factor COX18 acts transiently as a membrane insertase within the subunit 2 maturation module

Bourens¹,

Barrientos

2017

Journal of Biological Chemistry

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Edited by John M. Denu Defects in mitochondrial cytochrome c oxidase or respiratory chain complex IV (CIV) assembly are a frequent cause of human mitochondrial disorders. Specifically, mutations in four conserved assembly factors impinging the biogenesis of the mitochondrion-encoded catalytic core subunit 2 (COX2) result in myopathies. These factors afford stability of newly synthesized COX2 (the dystonia-ataxia syndrome protein COX20), a protein with two transmembrane domains, and maturation of its copper center, Cu A (cardiomyopathy proteins SCO1, SCO2, and COA6). COX18 is an additional COX2 assembly factor that belongs to the Oxa1 family of membrane protein insertases. Here, we used a gene-editing approach to generate a human COX18 knock-out HEK293T cell line that displays isolated complete CIV deficiency. We demonstrate that COX20 stabilizes COX2 during insertion of its N-proximal transmembrane domain, and subsequently, COX18 transiently interacts with COX2 to promote translocation across the inner membrane of the COX2 C-tail that contains the apo-Cu A site. The release of COX18 from this complex coincides with the binding of the SCO1-SCO2-COA6 copper metallation module to COX2-COX20 to finalize COX2 biogenesis. Therefore, COX18 is a new candidate when screening for mitochondrial disorders associated with isolated CIV deficiency.In nucleated human cells, mitochondria are central organelles that harbor the enzymes required for cellular respiration and aerobic energy production through oxidative phosphorylation (OXPHOS).2 These multimeric complexes are formed by subunits encoded in the nuclear and mitochondrial genomes that are assembled into functional units with the assistance of a myriad of nucleus-encoded ancillary proteins, generally called assembly factors. Mutations in OXPHOS subunits or assembly factors result in failure to fulfill the energy demands of most tissues with a major incidence in those with high energy

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“…Cox18 lacks such a ribosome-binding domain and interacts with translation products only after their Oxa1-mediated membrane insertion (12). Nevertheless, Cox18 also exhibits insertase activity because it functionally complements Escherichia coli mutants lacking YidC (17).…”

mentioning

confidence: 99%

Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function

Funes¹,

Hasona

Bauerschmitt³

et al. 2009

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

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YidC/Oxa/Alb3 family proteins catalyze the insertion of integral membrane proteins in bacteria, mitochondria, and chloroplasts, respectively. Unlike gram-negative organisms, gram-positive bacteria express 2 paralogs of this family, YidC1/SpoIIIJ and YidC2/ YgjG. In Streptococcus mutans, deletion of yidC2 results in a stress-sensitive phenotype similar to that of mutants lacking the signal recognition particle (SRP) protein translocation pathway, while deletion of yidC1 has a less severe phenotype. In contrast to eukaryotes and gram-negative bacteria, SRP-deficient mutants are viable in S. mutans; however, double SRP-yidC2 mutants are severely compromised. Thus, YidC2 may enable loss of the SRP by playing an independent but overlapping role in cotranslational protein insertion into the membrane. This is reminiscent of the situation in mitochondria that lack an SRP pathway and where Oxa1 facilitates cotranslational membrane protein insertion by binding directly to translation-active ribosomes. Here, we show that OXA1 complements a lack of yidC2 in S. mutans. YidC2 also functions reciprocally in oxa1-deficient Saccharomyces cerevisiae mutants and mediates the cotranslational insertion of mitochondrial translation products into the inner membrane. YidC2, like Oxa1, contains a positively charged C-terminal extension and associates with translating ribosomes. Our results are consistent with a gene-duplication event in gram-positive bacteria that enabled the specialization of a YidC isoform that mediates cotranslational activity independent of an SRP pathway. membrane protein insertion ͉ mitochondria ͉ Streptococcus mutans ͉ gram-positive bacteria ͉ ribosomes

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Saccharomyces cerevisiae Cox18 complements the essential Sec‐independent function of Escherichia coli YidC

Cited by 23 publications

References 49 publications

Bacillus subtilis SpoIIIJ and YqjG Function in Membrane Protein Biogenesis

Bacillus subtilis SpoIIIJ and YqjG Function in Membrane Protein Biogenesis

Human mitochondrial cytochrome c oxidase assembly factor COX18 acts transiently as a membrane insertase within the subunit 2 maturation module

Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function

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