Role of Surf1 in heme recruitment for bacterial COX biogenesis

Hannappel, Achim; Bundschuh, Freya A.; Ludwig, Bernd

doi:10.1016/j.bbabio.2011.09.007

Cited by 32 publications

(29 citation statements)

References 75 publications

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“…Surf1c and CtaA (heme A synthase; heme donor to Surf1c [16]) are exclusively observed in cross-linked membranes. CtaA is observed in the anti-COX-N and anti-COX-D elution fractions, while Surf1c is observed in the antiCtaG and anti-COX-N fractions.…”

Section: The Three Main Players In Cox Metallationmentioning

confidence: 99%

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Deciphering protein–protein interactions during the biogenesis of cytochrome c oxidase from Paracoccus denitrificans

Gurumoorthy

Ludwig

2014

The FEBS Journal

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Biogenesis of the mitochondrial cytochrome c oxidase (COX) is a complex process due to its numerous subunits encoded by two genomes, as well as the localization of redox centers deep within the membrane. Here, we have assessed the biogenesis of the homologous aa 3 -type oxidase of the soil bacterium Paracoccus denitrificans. First, protein partners were analyzed using various membrane solubilization strategies to show interactions between COX and CtaG, a chaperone implicated in Cu B site metallation. Using an unbiased MS approach after immunological pull-down from untreated or cross-linked membranes, we then extend our view towards a hypothetical 'biogenesis complex' by identifying two further metal-inserting chaperones, Surf1c and Sco, together with enzymes catalyzing heme a synthesis. Our study also tentatively supports previous speculation regarding the existence of a predominantly co-translational mechanism for cofactor insertion during COX biogenesis.

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Section: The Three Main Players In Cox Metallationmentioning

confidence: 99%

“…In mitochondria, physical association of Shy1 (the Surf1 homolog of yeast) and Cox15 in a biogenesis complex has been demonstrated [13][14][15]. Although the exact mechanism of incorporation of the heme molecules into SUI is still unknown, involvement of the Surf1c assembly factor has been shown in P. denitrificans [16,17].…”

Section: Introductionmentioning

confidence: 99%

Deciphering protein–protein interactions during the biogenesis of cytochrome c oxidase from Paracoccus denitrificans

Gurumoorthy

Ludwig

2014

The FEBS Journal

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“…The chaperone Surf1c is implicated in the insertion of heme into COX SUI [29]. Fig 1A shows two distinct spots at approximately 70 kDa and with higher staining intensity between 150 and 200 kDa.…”

Section: Resultsmentioning

confidence: 99%

“…The latter is a well-known COX biogenesis factor, whose functional loss is connected to Leigh syndrome in humans, a severe neurodegenerative disorder [22–24]. Even though the yeast homologue Shy1p is one of the best studied Surf1 homologues and found to interact with COX assembly intermediates [21, 25–27], studies in bacteria established its role as a heme a binding protein and its involvement in the hemylation of COX SUI [14, 28, 29]. …”

Section: Introductionmentioning

confidence: 99%

Cytochrome c Oxidase Biogenesis and Metallochaperone Interactions: Steps in the Assembly Pathway of a Bacterial Complex

et al. 2017

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Biogenesis of mitochondrial cytochrome c oxidase (COX) is a complex process involving the coordinate expression and assembly of numerous subunits (SU) of dual genetic origin. Moreover, several auxiliary factors are required to recruit and insert the redox-active metal compounds, which in most cases are buried in their protein scaffold deep inside the membrane. Here we used a combination of gel electrophoresis and pull-down assay techniques in conjunction with immunostaining as well as complexome profiling to identify and analyze the composition of assembly intermediates in solubilized membranes of the bacterium Paracoccus denitrificans. Our results show that the central SUI passes through at least three intermediate complexes with distinct subunit and cofactor composition before formation of the holoenzyme and its subsequent integration into supercomplexes. We propose a model for COX biogenesis in which maturation of newly translated COX SUI is initially assisted by CtaG, a chaperone implicated in CuB site metallation, followed by the interaction with the heme chaperone Surf1c to populate the redox-active metal-heme centers in SUI. Only then the remaining smaller subunits are recruited to form the mature enzyme which ultimately associates with respiratory complexes I and III into supercomplexes.

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“…Besides the prosthetic groups mentioned, RMPs depend on specific catalytic metals (Cu, Fe). The acquirement of these metals, usually at the periplasm, and insertion into the subunits is mediated by enzyme-specific chaperones (Abicht et al, 2014;Dash, Alles, Bundschuh, Richter, & Ludwig, 2015;Hannappel, Bundschuh, & Ludwig, 2012;Robinson & Winge, 2010). All in all, enzyme maturation is highly complex, wherein each RMP depends on its dedicated set of assembly factors acting in concert.…”

Section: Assembly Of Bacterial Respiratory Complexesmentioning

confidence: 99%

Bacterial Electron Transfer Chains Primed by Proteomics

Wessels¹,

Almeida²,

Kartal³

et al. 2016

Advances in Bacterial Electron Transport Systems and Their Regulation

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Electron transport phosphorylation is the central mechanism for most prokaryotic species to harvest energy released in the respiration of their substrates as ATP. Microorganisms have evolved incredible variations on this principle, most of these we perhaps do not know, considering that only a fraction of the microbial richness is known. Besides these variations, microbial species may show substantial versatility in using respiratory systems. In connection herewith, regulatory mechanisms control the expression of these respiratory enzyme systems and their assembly at the translational and posttranslational levels, to optimally accommodate changes in the supply of their energy substrates. Here, we present an overview of methods and techniques from the field of proteomics to explore bacterial electron transfer chains and their regulation at levels ranging from the whole organism down to the Ångstrom scales of protein structures. From the survey of the literature on this subject, it is concluded that proteomics, indeed, has substantially contributed to our comprehending of bacterial respiratory mechanisms, often in elegant combinations with genetic and biochemical approaches. However, we also note that advanced proteomics offers a wealth of opportunities, which have not been exploited at all, or at best underexploited in hypothesis-driving and hypothesis-driven research on bacterial bioenergetics. Examples obtained from the related area of mitochondrial oxidative phosphorylation research, where the application of advanced proteomics is more common, may illustrate these opportunities.

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Role of Surf1 in heme recruitment for bacterial COX biogenesis

Cited by 32 publications

References 75 publications

Deciphering protein–protein interactions during the biogenesis of cytochrome c oxidase from Paracoccus denitrificans

Deciphering protein–protein interactions during the biogenesis of cytochrome c oxidase from Paracoccus denitrificans

Cytochrome c Oxidase Biogenesis and Metallochaperone Interactions: Steps in the Assembly Pathway of a Bacterial Complex

Bacterial Electron Transfer Chains Primed by Proteomics

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