Porins from plants. Molecular cloning and functional characterization of two new members of the porin family.

Fischer, Karsten; Weber, Andreas; Brink, Susanne; Arbinger, Bettina; Schünemann, Danja; Borchert, Sieglinde; Heldt, Hans W.; Popp, Birgit; Benz, Roland; Link, Thomas

doi:10.1016/s0021-9258(18)47312-7

Cited by 86 publications

(28 citation statements)

References 32 publications

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“…Membrane proteins (MPs) play a key role in many biological processes, such as cell recognition, signal transmission, enzymatic reactions, and transport of metabolites. − Their importance is proved by the fact that 50% of medical drugs are currently on the marked target MPs. − The structure of MPs is restricted to α-helix and β-barrel due to the need to satisfy all hydrogen bonds within the water-excluded native bilayer environment. Although α-helical MPs are present in most biological membranes, β-barrel MPs are exclusively found in the outer membranes (OM) of Gram-negative bacteria and eukaryotic organelles directly derived from prokaryotic ancestors, namely, mitochondria and chloroplasts …”

Section: Introductionmentioning

confidence: 99%

Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes

et al. 2018

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Omp2a β-barrel outer membrane protein has been reconstituted into supported lipid bilayers (SLBs) to compare the nanomechanical properties (elastic modulus, adhesion forces, and deformation) and functionality of the resulting bioinspired system with those of Omp2a-based polymeric nanomembranes (NMs). Protein reconstitution into lipid bilayers has been performed using different strategies, the most successful one consisting of a detergent-mediated process into preformed liposomes. The elastic modulus obtained for the lipid bilayer and Omp2a are ∼19 and 10.5 ± 1.7 MPa, respectively. Accordingly, the protein is softer than the lipid bilayer, whereas the latter exhibits less mechanical strength than polymeric NMs. Besides, the function of Omp2a in the SLB is similar to that observed for Omp2a-based polymeric NMs. Results open the door to hybrid bioinspired substrates based on the integration of Omp2a-proteoliposomes and nanoperforated polymeric freestanding NMs.

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Section: Introductionmentioning

confidence: 99%

Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes

et al. 2018

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“…binding is that this particular lysine residue (Figure 2B) ) and the mitochondrial porins of Neurospora crassa (NC), S. cerevisiae (SC), and D. discoideum (DD) (Troll et al, 1992;Fischer et al, 1994) were aligned to the first GLK of PorB of Ngo strains VPI (P.IA) and R16 (P.IB).…”

Section: Introductionmentioning

confidence: 99%

“…Sequence Alignment of Putative ATP/GTP-Binding Motifs in Neisserial PorB and Other ATP-or GTP-Binding Proteins(A) Comparison with eukaryotic porins. GLK motives and adjacent amino acids of human 31HL porin (human 31HL) and the mitochondrial porins of Neurospora crassa (NC), S. cerevisiae (SC), and D. discoideum (DD)(Troll et al., 1992;Fischer et al, 1994) were aligned to the first GLK of PorB of Ngo strains VPI (P.IA) and R16 (P.IB). (B) Comparison of the second GLK motif of PorB with a known GTP-binding site in the TCR subunit(Peter et al, 1992).…”

mentioning

confidence: 99%

Modulation of Neisseria Porin (PorB) by Cytosolic ATP/GTP of Target Cells: Parallels between Pathogen Accommodation and Mitochondrial Endosymbiosis

Rudel

Schmid

Benz

et al. 1996

Cell

123

128

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PorB of the pathogenic Neisseria species belongs to the large family of pore-forming proteins (porins) produced by gram-negative bacteria. PorB is exceptional in that it is capable of translocating vectorially into membranes of infected target cells and functions in the infection process. Here we report on an unexpected similarity between Neisserial PorB and mitochondrial porins. Both porin classes interact with purine nucleoside triphosphates, which down-regulate pore size and cause a shift in voltage dependence and ion selectivity. Patch-clamp analyses indicate that PorB channel activity is tightly regulated in intact epithelial cells. In light of recent findings on the pivotal role of PorB in virulence and the prevention of phagosome lysosome fusion, these data provide important mechanistic clues on the intracellular pathogen accommodation reminiscent of mitochondrial endosymbiosis.

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“…The voltage dependence of eukaryotic porins from a variety of eukaryotic organisms was investigated in detail in many studies: Paramecium ( Schein et al, 1976 ; Doring and Colombini, 1984 ; Ludwig et al, 1989 ); Mammals: rat ( Roos et al, 1982 ; Colombini, 1983 ; Ludwig et al, 1986 ), rabbit ( De Pinto et al, 1987a ), bovine ( De Pinto et al, 1987a ), pig ( De Pinto et al, 1987a ), and human brain ( Bureau et al, 1992 ); Fish: Anguilla anguilla ( De Pinto et al, 1991c ); Plants: potato ( Heins et al, 1994 ; Lopes-Rodrigues et al, 2020 ), pea ( Fischer et al, 1994 ), corn ( Smack and Colombini, 1985 ; Aljamal et al, 1993 ; Fischer et al, 1994 ), wheat ( Blumenthal et al, 1993 ), and pea root plastid porin ( Fischer et al, 1994 ; Popp et al, 1997 ); Other organisms: Neurospora crassa ( Freitag et al, 1982c ), yeast ( Ludwig et al, 1988 ), and Dictyostelium ( Troll et al, 1992 ); and Flies: Protophormia ( Wiesner et al, 1996 ) and Drosophila ( De Pinto et al, 1989a ; Aiello et al, 2004 ; Komarov et al, 2004 ). Common to all of these studies is that the eukaryotic porins of all these eukaryotes formed high-conducting channels in reconstituted systems.…”

Section: A Voltage-dependent Pore Was Discovered In Crude Extracts Of...mentioning

confidence: 99%

Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century

Benz

2021

Front. Physiol.

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Eukaryotic porin, also known as Voltage-Dependent Anion Channel (VDAC), is the most frequent protein in the outer membrane of mitochondria that are responsible for cellular respiration. Mitochondria are most likely descendants of strictly aerobic Gram-negative bacteria from the α-proteobacterial lineage. In accordance with the presumed ancestor, mitochondria are surrounded by two membranes. The mitochondrial outer membrane contains besides the eukaryotic porins responsible for its major permeability properties a variety of other not fully identified channels. It encloses also the TOM apparatus together with the sorting mechanism SAM, responsible for the uptake and assembly of many mitochondrial proteins that are encoded in the nucleus and synthesized in the cytoplasm at free ribosomes. The recognition and the study of electrophysiological properties of eukaryotic porin or VDAC started in the late seventies of the last century by a study of Schein et al., who reconstituted the pore from crude extracts of Paramecium mitochondria into planar lipid bilayer membranes. Whereas the literature about structure and function of eukaryotic porins was comparatively rare during the first 10years after the first study, the number of publications started to explode with the first sequencing of human Porin 31HL and the recognition of the important function of eukaryotic porins in mitochondrial metabolism. Many genomes contain more than one gene coding for homologs of eukaryotic porins. More than 100 sequences of eukaryotic porins are known to date. Although the sequence identity between them is relatively low, the polypeptide length and in particular, the electrophysiological characteristics are highly preserved. This means that all eukaryotic porins studied to date are anion selective in the open state. They are voltage-dependent and switch into cation-selective substates at voltages in the physiological relevant range. A major breakthrough was also the elucidation of the 3D structure of the eukaryotic pore, which is formed by 19 β-strands similar to those of bacterial porin channels. The function of the presumed gate an α-helical stretch of 20 amino acids allowed further studies with respect to voltage dependence and function, but its exact role in channel gating is still not fully understood.

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Porins from plants. Molecular cloning and functional characterization of two new members of the porin family.

Cited by 86 publications

References 32 publications

Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes

Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes

Modulation of Neisseria Porin (PorB) by Cytosolic ATP/GTP of Target Cells: Parallels between Pathogen Accommodation and Mitochondrial Endosymbiosis

Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century

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