Assembly of outer-membrane proteins in bacteria and mitochondria
Tóm tắt
The cell envelope of Gram-negative bacteria consists of two membranes separated by the periplasm. In contrast with most integral membrane proteins, which span the membrane in the form of hydrophobic
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Tài liệu tham khảo
Agterberg, 1990, Outer-membrane PhoE protein of Escherichia coli K-12 as an exposure vector: possibilities and limitations, Gene, 88, 37, 10.1016/0378-1119(90)90057-X
Anwari, 2010, A modular BAM complex in the outer membrane of the α-proteobacterium Caulobacter crescentus, PLoS One, 5, e8619, 10.1371/journal.pone.0008619
Bayrhuber, 2008, Structure of the human voltage-dependent anion channel, Proc Natl Acad Sci U S A, 105, 15370, 10.1073/pnas.0808115105
Behrens, 2001, The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity, EMBO J, 20, 285, 10.1093/emboj/20.1.285
Bos, 2004, Identification of an outer membrane protein required for lipopolysaccharide transport to the bacterial cell surface, Proc Natl Acad Sci U S A, 101, 9417, 10.1073/pnas.0402340101
Bos, 2007a, Biogenesis of the Gram-negative bacterial outer membrane, Annu Rev Microbiol, 61, 191, 10.1146/annurev.micro.61.080706.093245
Bos, 2007b, Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain, EMBO Rep, 8, 1149, 10.1038/sj.embor.7401092
Bosch, 1988, Export and localization of N-terminally truncated derivatives of Escherichia coli K-12 outer membrane protein PhoE, J Biol Chem, 263, 9952, 10.1016/S0021-9258(19)81610-1
Chacinska, 2009, Importing mitochondrial proteins: machineries and mechanisms, Cell, 138, 628, 10.1016/j.cell.2009.08.005
Chen, 1996, A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins, Mol Microbiol, 19, 1287, 10.1111/j.1365-2958.1996.tb02473.x
Costanzo, 2006, Growth phase-dependent regulation of the extracytoplasmic stress factor, σE, by guanosine 3′,5′-bipyrophosphate (ppGpp, J Bacteriol, 188, 4627, 10.1128/JB.01981-05
de Cock, 1997, Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12, J Mol Biol, 269, 473, 10.1006/jmbi.1997.1069
de Cock, 1999, Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein, Eur J Biochem, 259, 96, 10.1046/j.1432-1327.1999.00010.x
Dekker, 1995, In vitro folding of Escherichia coli outer-membrane phospholipase A, Eur J Biochem, 232, 214, 10.1111/j.1432-1033.1995.tb20801.x
Driessen, 2008, Protein translocation across the bacterial cytoplasmic membrane, Annu Rev Biochem, 77, 643, 10.1146/annurev.biochem.77.061606.160747
Fardini, 2009, Investigation of the role of the BAM complex and SurA chaperone in outer membrane protein biogenesis and T3SS expression in Salmonella, Microbiology, 155, 1613, 10.1099/mic.0.025155-0
Fussenegger, 1996, A novel peptidoglycan-linked lipoprotein (ComL) that functions in natural transformation competence of Neisseria gonorrhoeae, Mol Microbiol, 19, 1095, 10.1046/j.1365-2958.1996.457984.x
Gatsos, 2008, Protein secretion and outer membrane assembly in Alphaproteobacteria, FEMS Microbiol Rev, 32, 995, 10.1111/j.1574-6976.2008.00130.x
Gatzeva-Topalova, 2008, Crystal structure of YaeT: conformational flexibility and substrate recognition, Structure, 16, 1873, 10.1016/j.str.2008.09.014
Gentle, 2004, The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria, J Cell Biol, 164, 19, 10.1083/jcb.200310092
Habib, 2007, The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial β-barrel proteins, J Cell Biol, 176, 77, 10.1083/jcb.200602050
Harms, 2001, The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane, J Biol Chem, 276, 18804, 10.1074/jbc.M011194200
Hiller, 2008, Solution structure of the integral human membrane protein VDAC-1 in detergent micelles, Science, 321, 1206, 10.1126/science.1161302
Hsu, 2009, Two evolutionarily conserved essential β-barrel proteins in the chloroplast outer envelope membrane, Biosci Trends, 3, 168
Ishikawa, 2004, Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly, J Cell Biol, 166, 621, 10.1083/jcb.200405138
Johansen, 2006, Conserved small non-coding RNAs that belong to the σE regulon: role in down-regulation of outer membrane proteins, J Mol Biol, 364, 1, 10.1016/j.jmb.2006.09.004
Kim, 2007, Structure and function of an essential component of the outer membrane protein assembly machine, Science, 317, 961, 10.1126/science.1143993
Knowles, 2008, Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes, Mol Microbiol, 68, 1216, 10.1111/j.1365-2958.2008.06225.x
Koebnik, 2000, Structure and function of bacterial outer membrane proteins: barrels in a nutshell, Mol Microbiol, 37, 239, 10.1046/j.1365-2958.2000.01983.x
Korndörfer, 2004, Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture, Nat Struct Mol Biol, 11, 1015, 10.1038/nsmb828
Kozjak, 2003, An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane, J Biol Chem, 278, 48520, 10.1074/jbc.C300442200
Krimmer, 2001, Biogenesis of the major mitochondrial outer membrane protein porin involves a complex import pathway via receptors and the general import pore, J Cell Biol, 152, 289, 10.1083/jcb.152.2.289
Krojer, 2008, Structural basis for the regulated protease and chaperone function of DegP, Nature, 453, 885, 10.1038/nature07004
Kutik, 2008, Dissecting membrane insertion of mitochondrial β-barrel proteins, Cell, 132, 1011, 10.1016/j.cell.2008.01.028
Lazar, 1996, SurA assists the folding of Escherichia coli outer membrane proteins, J Bacteriol, 178, 1770, 10.1128/JB.178.6.1770-1773.1996
Malinverni, 2006, YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli, Mol Microbiol, 61, 151, 10.1111/j.1365-2958.2006.05211.x
Manning, 1998, Omp85 of Neisseria gonorrhoeae and Neisseria meningitidis are similar to Haemophilus influenzae D-15-Ag and Pasteurella multocida Oma87, Microb Pathog, 25, 11, 10.1006/mpat.1998.0206
Milenkovic, 2004, Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability, J Biol Chem, 279, 22781, 10.1074/jbc.C400120200
Model, 2001, Multistep assembly of the protein import channel of the mitochondrial outer membrane, Nat Struct Biol, 8, 361, 10.1038/86253
Nakamura, 1976, Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12, J Biochem, 80, 1411, 10.1093/oxfordjournals.jbchem.a131414
Nikaido, 2003, Molecular basis of bacterial outer membrane permeability revisited, Microbiol Mol Biol Rev, 67, 593, 10.1128/MMBR.67.4.593-656.2003
Papenfort, 2006, σE-dependent small RNAs of Salmonella respond to membrane stress by accelerating global omp mRNA decay, Mol Microbiol, 62, 1674, 10.1111/j.1365-2958.2006.05524.x
Paschen, 2003, Evolutionary conservation of biogenesis of β-barrel membrane proteins, Nature, 426, 862, 10.1038/nature02208
Rapaport, 1999, Biogenesis of Tom40, core component of the TOM complex of mitochondria, J Cell Biol, 146, 321, 10.1083/jcb.146.2.321
Reumann, 1999, The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog, Proc Natl Acad Sci U S A, 96, 784, 10.1073/pnas.96.2.784
Rizzitello, 2001, Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli, J Bacteriol, 183, 6794, 10.1128/JB.183.23.6794-6800.2001
Robert, 2006, Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif, PLoS Biol, 4, e377, 10.1371/journal.pbio.0040377
Rouvière, 1996, SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins, Genes Dev, 10, 3170, 10.1101/gad.10.24.3170
Ruiz, 2005, Sensing external stress: watchdogs of the Escherichia coli cell envelope, Curr Opin Microbiol, 8, 122, 10.1016/j.mib.2005.02.013
Rutten, 2009, Active-site architecture and catalytic mechanism of the lipid A deacylase LpxR of Salmonella typhimurium, Proc Natl Acad Sci U S A, 106, 1960, 10.1073/pnas.0813064106
Sánchez-Pulido, 2003, POTRA: a conserved domain in the FtsQ family and a class of β-barrel outer membrane proteins, Trends Biochem Sci, 28, 523, 10.1016/j.tibs.2003.08.003
Schäfer, 1999, Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins, J Biol Chem, 274, 24567, 10.1074/jbc.274.35.24567
Sklar, 2007a, Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli, Proc Natl Acad Sci U S A, 104, 6400, 10.1073/pnas.0701579104
Sklar, 2007b, Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli, Genes Dev, 21, 2473, 10.1101/gad.1581007
Spiess, 1999, A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein, Cell, 97, 339, 10.1016/S0092-8674(00)80743-6
Steeghs, 2001, Outer membrane composition of a lipopolysaccharide-deficient Neisseria meningitidis mutant, EMBO J, 20, 6937, 10.1093/emboj/20.24.6937
Stegmeier, 2006, Characterization of pores formed by YaeT (Omp85) from Escherichia coli, J Biochem, 140, 275, 10.1093/jb/mvj147
Struyvé, 1991, Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein, J Mol Biol, 218, 141, 10.1016/0022-2836(91)90880-F
Tam, 2005, Changes in lipopolysaccharide structure induce the σE-dependent response of Escherichia coli, Mol Microbiol, 55, 1403, 10.1111/j.1365-2958.2005.04497.x
Tefsen, 2005, MsbA is not required for phospholipid transport in Neisseria meningitidis, J Biol Chem, 280, 35961, 10.1074/jbc.M509026200
Thomas, 2001, Cloning, overexpression, purification, and immunobiology of an 85-kilodalton outer membrane protein from Haemophilus ducreyi, Infect Immun, 69, 4438, 10.1128/IAI.69.7.4438-4446.2001
Tsukazaki, 2008, Conformational transition of Sec machinery inferred from bacterial SecYE structures, Nature, 455, 988, 10.1038/nature07421
Ujwal, 2008, The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating, Proc Natl Acad Sci U S A, 105, 17742, 10.1073/pnas.0809634105
Vertommen, 2009, Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics, Proteomics, 9, 2432, 10.1002/pmic.200800794
Volokhina, 2009, The β-barrel outer membrane protein assembly complex of Neisseria meningitidis, J Bacteriol, 191, 7074, 10.1128/JB.00737-09
Voulhoux, 2004, Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly, Res Microbiol, 155, 129, 10.1016/j.resmic.2003.11.007
Voulhoux, 2003, Role of a highly conserved bacterial protein in outer membrane protein assembly, Science, 299, 262, 10.1126/science.1078973
Waizenegger, 2004, Tob38, a novel essential component in the biogenesis of β-barrel proteins of mitochondria, EMBO Rep, 5, 704, 10.1038/sj.embor.7400183
Walther, 2009, Biogenesis of mitochondrial outer membrane proteins, Biochim Biophys Acta, 1793, 42, 10.1016/j.bbamcr.2008.04.013
Walther, 2009a, Signals in bacterial β-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria, Proc Natl Acad Sci U S A, 106, 2531, 10.1073/pnas.0807830106
Walther, 2009b, Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence, Cell Mol Life Sci, 66, 2789, 10.1007/s00018-009-0029-z
Walther, 2010, The mitochondrial porin, VDAC, has retained the ability to be assembled in the bacterial outer membrane, Mol Biol Evol, 27, 887, 10.1093/molbev/msp294
Walton, 2004, Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation, Mol Cell, 15, 367, 10.1016/j.molcel.2004.07.023
Walton, 2009, The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains, Proc Natl Acad Sci U S A, 106, 1772, 10.1073/pnas.0809275106
Wiedemann, 2003, Machinery for protein sorting and assembly in the mitochondrial outer membrane, Nature, 424, 565, 10.1038/nature01753