Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity.

Saavedra-Alanís, Víctor; Ryšavý, P.; Rosenberg, León E.; Kalousek, František

doi:10.1016/s0021-9258(17)37105-3

Cited by 58 publications

(5 citation statements)

References 35 publications

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“…While most of these were in relatively low abundance, even with the bait with which they scored, some of these proximity interactors were more notable. PMPCA, as a bait, strongly and specifically enriched PMPCB (Figure 2D), its binding partner in the mitochondrial processing peptidase complex (Saavedra-Alanis et al, 1994). Another example is the proximity interaction between MCU (mitochondrial calcium uniporter) and MCUB, which form the complex responsible for Ca 2+ import into mitochondrial matrix (Raffaello et al, 2013) (Figure 2D).…”

Section: A Comprehensive Exploration Of Mitochondria By Bioidmentioning

confidence: 97%

A High-Density Human Mitochondrial Proximity Interaction Network

et al. 2020

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Section: A Comprehensive Exploration Of Mitochondria By Bioidmentioning

confidence: 97%

A High-Density Human Mitochondrial Proximity Interaction Network

et al. 2020

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“…Moreover, MBP enhances solubility so strongly that it can even solubilize unfolded/misfolded proteins. In these cases, the target proteins often precipitate after enzymatic cleavage of MBP, resulting in wasted time and resources (Lee et al, 1993;Saavedraalanis et al, 1994;Kishore et al, 1998). In order to verify that MBP facilitates the production of folded, active protein, and does not simply solubilize misfolded proteins, it is advantageous to coexpress the MBP fusion protein with its sitespecific protease.…”

Section: 2413mentioning

confidence: 99%

Strategies to Optimize Protein Expression in E. coli

2010

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Recombinant protein expression in Escherichia coli (E. coli) is simple, fast, inexpensive, and robust, with the expressed protein comprising up to 50 percent of the total cellular protein. However, it also has disadvantages. For example, the rapidity of bacterial protein expression often results in unfolded/misfolded proteins, especially for heterologous proteins that require longer times and/or molecular chaperones to fold correctly. In addition, the highly reductive environment of the bacterial cytosol and the inability of E. coli to perform several eukaryotic post-translational modifications results in the insoluble expression of proteins that require these modifications for folding and activity. Fortunately, multiple, novel reagents and techniques have been developed that allow for the efficient, soluble production of a diverse range of heterologous proteins in E. coli. This overview describes variables at each stage of a protein expression experiment that can influence solubility and offers a summary of strategies used to optimize soluble expression in E. coli.

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“…Cor2 subunit of CIII 2 , located adjacent to Cor1, is homologous to the α-subunit of MPP ( 38 , 61 , 62 ). Even though β-MPP harbors the Zn 2+ -containing catalytic site, this subunit has low activity in the absence of the α-MPP subunit ( 63 – 65 ).…”

Section: Resultsmentioning

confidence: 99%

Structure and function of theS. pombeIII–IV–cytcsupercomplex

Moe,

Dimogkioka,

Rapaport

et al. 2023

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

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The respiratory chain in aerobic organisms is composed of a number of membrane-bound protein complexes that link electron transfer to proton translocation across the membrane. In mitochondria, the final electron acceptor, complex IV (CIV), receives electrons from dimeric complex III (CIII2), via a mobile electron carrier, cytochromec. In the present study, we isolated the CIII2CIV supercomplex from the fission yeastSchizosaccharomyces pombeand determined its structure with bound cyt.cusing single-particle electron cryomicroscopy. A respiratory supercomplex factor 2 was found to be bound at CIV distally positioned in the supercomplex. In addition to the redox-active metal sites, we found a metal ion, presumably Zn2+, coordinated in the CIII subunit Cor1, which is encoded by the same gene (qcr1) as the mitochondrial-processing peptidase subunit β. Our data show that the isolated CIII2CIV supercomplex displays proteolytic activity suggesting a dual role of CIII2inS. pombe. As in the supercomplex fromS. cerevisiae, subunit Cox5 of CIV faces towards one CIII monomer, but inS. pombe,the two complexes are rotated relative to each other by ~45°. This orientation yields equal distances between the cyt.cbinding sites at CIV and at each of the two CIII monomers. The structure shows cyt.cbound at four positions, but only along one of the two symmetrical branches. Overall, this combined structural and functional study reveals the integration of peptidase activity with the CIII2respiratory system and indicates a two-dimensional cyt.cdiffusion mechanism within the CIII2–CIV supercomplex.

show abstract

Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity.

Cited by 58 publications

References 35 publications

A High-Density Human Mitochondrial Proximity Interaction Network

A High-Density Human Mitochondrial Proximity Interaction Network

Strategies to Optimize Protein Expression in E. coli

Structure and function of theS. pombeIII–IV–cytcsupercomplex

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