The Proline-rich Antibacterial Peptide Bac7 Binds to and Inhibits in vitro the Molecular Chaperone DnaK
Tóm tắt
Từ khóa
Tài liệu tham khảo
Agerberth B, Lee JY, Bergman T et al (1991) Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur J Biochem 202:849–854
Benincasa M, Scocchi M, Podda E et al (2004) Antimicrobial activity of Bac7 fragments against drug-resistant clinical isolates. Peptides 25:2055–2061
Bischofberger P, Han W, Feifel B, Schonfeld HJ, Christen P (2003) D-Peptides as inhibitors of the DnaK/DnaJ/GrpE chaperone system. J Biol Chem 278:19044–19047
Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3:238–250
Bulaj G, Kortemme T, Goldenberg DP (1998) Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry 37:8965–8972
Casteels P, Ampe C, Jacobs F, Vaeck M, Tempst P (1989) Apidaecins: antibacterial peptides from honeybees. EMBO J 8:2387–2391
Chan YR, Gallo RL (1998) PR-39, a syndecan-inducing antimicrobial peptide, binds and affects p130(Cas). J Biol Chem 273:28978–28985
Chesnokova LS, Slepenkov SV, Witt SN (2004) The insect antimicrobial peptide, l-pyrrhocoricin, binds to and stimulates the ATPase activity of both wild-type and lidless DnaK. FEBS Lett 565:65–69
Cho JH, Park CB, Yoon YG, Kim SC (1998) Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization. Biochim Biophys Acta 1408:67–76
Cudic M, Otvos L Jr (2002) Intracellular targets of antibacterial peptides. Curr Drug Targets 3:101–106
Destoumieux D, Bulet P, Loew D et al (1997) Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J Biol Chem 272:28398–28406
Feifel B, Sandmeier E, Schonfeld HJ, Christen P (1996) Potassium ions and the molecular-chaperone activity of DnaK. Eur J Biochem 237:318–321
Feifel B, Schonfeld HJ, Christen P (1998) D-peptide ligands for the co-chaperone DnaJ. J Biol Chem 273:11999–12002
Frank RW, Gennaro R, Schneider K, Przybylski M, Romeo D (1990) Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J Biol Chem 265:18871–18874
Gaczynska M, Osmulski PA, Gao Y, Post MJ, Simons M (2003) Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 42:8663–8670
Gallo RL, Ono M, Povsic T et al (1994) Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc Natl Acad Sci USA 91:11035–11039
Gennaro R, Skerlavaj B, Romeo D (1989) Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect Immun 57:3142–3146
Gennaro R, Scocchi M, Merluzzi L, Zanetti M (1998) Biological characterization of a novel mammalian antimicrobial peptide. Biochim Biophys Acta 1425:361–368
Gennaro R, Zanetti M, Benincasa M, Podda E, Miani M (2002) Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action. Curr Pharm Des 8:763–778
Hale JD, Hancock RE (2007) Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev Anti Infect Ther 5:951–959
Han W, Christen P (2003) Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system. J Biol Chem 278:19038–19043
Hartl FU, Martin J, Neupert W (1992) Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annu Rev Biophys Biomol Struct 21:293–322
Kay BK, Williamson MP, Sudol M (2000) The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J 14:231–241
Kragol G, Lovas S, Varadi G et al (2001) The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry 40:3016–3026
Kragol G, Hoffmann R, Chattergoon MA et al (2002) Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin. Eur J Biochem 269:4226–4237
Laufen T, Mayer MP, Beisel C et al (1999) Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci USA 96:5452–5457
Liebscher M, Roujeinikova A (2009) Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies. J Bacteriol 191:1456–1462
Liebscher M, Jahreis G, Lucke C et al (2007) Fatty acyl benzamido antibacterials based on inhibition of DnaK-catalyzed protein folding. J Biol Chem 282:4437–4446
Liu X (2002) Concentrations of the GroEL/GroES and the DnaK/DnaJ/GrpE molecular chaperones in Escherichia coli under normal and heat shock conditions. M.D. thesis. Universität Zürich, Zürich, Switzerland
Mattiuzzo M, Bandiera A, Gennaro R et al (2007) Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides. Mol Microbiol 66:151–163
Mogk A, Tomoyasu T, Goloubinoff P et al (1999) Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18:6934–6949
Osborn MJ, Munson R (1974) Separation of the inner (cytoplasmic) and outer membranes of gram-negative bacteria. Methods Enzymol 31:642–653
Otvos L Jr (2002) The short proline-rich antibacterial peptide family. Cell Mol Life Sci 59:1138–1150
Otvos L Jr, Rogers ME, Consolvo PJ et al (2000) Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39:14150–14159
Pierpaoli EV, Gisler SM, Christen P (1998) Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Biochemistry 37:16741–16748
Podda E, Benincasa M, Pacor S et al (2006) Dual mode of action of Bac7, a proline-rich antibacterial peptide. Biochim Biophys Acta 1760:1732–1740
Reddy KV, Yedery RD, Aranha C (2004) Antimicrobial peptides: premises and promises. Int J Antimicrob Agents 24:536–547
Rudiger S, Germeroth L, Schneider-Mergener J, Bukau B (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J 16:1501–1507
Rudiger S, Schneider-Mergener J, Bukau B (2001) Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 20:1042–1050
Schmid D, Baici A, Gehring H, Christen P (1994) Kinetics of molecular chaperone action. Science 263:971–973
Schonfeld HJ, Schmidt D, Schroder H, Bukau B (1995a) The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J Biol Chem 270:2183–2189
Schonfeld HJ, Schmidt D, Zulauf M (1995b) Investigation of the molecular chaperone DnaJ by analytical ultracentrifugation. Prog Colloid Polym Sci 99:7–10
Shamova O, Brogden KA, Zhao C et al (1999) Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes. Infect Immun 67:4106–4111
Shi J, Ross CR, Leto TL, Blecha F (1996) PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox. Proc Natl Acad Sci USA 93:6014–6018
Stensvag K, Haug T, Sperstad SV et al (2008) Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. Dev Comp Immunol 32:275–285
Tomasinsig L, Zanetti M (2005) The cathelicidins: structure, function and evolution. Curr Protein Pept Sci 6:23–34
Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B (2001) Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol 40:397–413
Zhang L, Falla TJ (2006) Antimicrobial peptides: therapeutic potential. Expert Opin Pharmacother 7:653–663