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Volumn 6, Issue , 2015, Pages

Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase

Author keywords

[No Author keywords available]

Indexed keywords

CYCLASE; CYCLOTIDE; CYSTEINE PROTEINASE; LEGUMAIN; OLDENLANDIA AFFINIS ASPARAGINYL ENDOPEPTIDASE B; PEPTIDE DERIVATIVE; PROTEINASE; RECOMBINANT ASPARAGINYL ENDOPEPTIDASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; MESSENGER RNA; PEPTIDE; PLANT PROTEIN;

EID: 84951824827     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10199     Document Type: Article
Times cited : (191)

References (48)
  • 1
    • 0030456404 scopus 로고    scopus 로고
    • Post-translational peptide bond formation during conconavalin A processing in vitro
    • Sheldon, P. S., Keen, J. N. & Bowles, D. J. Post-translational peptide bond formation during conconavalin A processing in vitro. Biochem. J. 320, 865-870 (1996).
    • (1996) Biochem. J. , vol.320 , pp. 865-870
    • Sheldon, P.S.1    Keen, J.N.2    Bowles, D.J.3
  • 2
    • 1142269466 scopus 로고    scopus 로고
    • Immune recognition of a human renal cancer antigen through post-translational protein splicing
    • Hanada, K., Yewdell, J. W. & Yang, J. C. Immune recognition of a human renal cancer antigen through post-translational protein splicing. Nature 427, 1-5 (2004).
    • (2004) Nature , vol.427 , pp. 1-5
    • Hanada, K.1    Yewdell, J.W.2    Yang, J.C.3
  • 3
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus Sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S. K., Liu, G., Ton-That, H. & Schneewind, O. Staphylococcus aureus Sortase, an enzyme that anchors surface proteins to the cell wall. Science 285, 760-763 (1999).
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 4
    • 84877149384 scopus 로고    scopus 로고
    • The two-step biosynthesis of cyclic peptides from linear precursors in a member of the plant family Caryophyllaceae involves cyclization by a serine protease-like enzyme
    • Barber, C. J. S. et al. The two-step biosynthesis of cyclic peptides from linear precursors in a member of the plant family Caryophyllaceae involves cyclization by a serine protease-like enzyme. J. Biol. Chem. 288, 12500-12510 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 12500-12510
    • Barber, C.J.S.1
  • 5
    • 84906318100 scopus 로고    scopus 로고
    • Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis
    • Nguyen, G. K. T. et al. Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis. Nat. Chem. Biol. 10, 732-738 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 732-738
    • Nguyen, G.K.T.1
  • 6
    • 84919903118 scopus 로고    scopus 로고
    • Peptide macrocyclization catalyzed by a prolyl oligopeptidase involved in a-amanitin biosynthesis
    • Luo, H. et al. Peptide macrocyclization catalyzed by a prolyl oligopeptidase involved in a-amanitin biosynthesis. Chem. Biol. 21, 1610-1617 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 1610-1617
    • Luo, H.1
  • 7
    • 67749142086 scopus 로고    scopus 로고
    • Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates
    • Lee, J., Mcintosh, J., Hathaway, B. J. & Schmidt, E. W. Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates. J. Am. Chem. Soc. 131, 2122-2124 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2122-2124
    • Lee, J.1    McIntosh, J.2    Hathaway, B.J.3    Schmidt, E.W.4
  • 8
    • 38649136638 scopus 로고    scopus 로고
    • Biosynthesis of circular proteins in plants
    • Gillon, A. D. et al. Biosynthesis of circular proteins in plants. Plant J. 53, 505-515 (2008).
    • (2008) Plant J. , vol.53 , pp. 505-515
    • Gillon, A.D.1
  • 9
    • 35748954039 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase mediates in vivo protein backbone cyclization
    • Saska, I. et al. An asparaginyl endopeptidase mediates in vivo protein backbone cyclization. J. Biol. Chem. 282, 29721-29728 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 29721-29728
    • Saska, I.1
  • 10
    • 84930085736 scopus 로고    scopus 로고
    • Peptide macrocyclization by a bifunctional endoprotease
    • Bernath-Levin, K. et al. Peptide macrocyclization by a bifunctional endoprotease. Chem. Biol. 22, 571-582 (2015).
    • (2015) Chem. Biol. , vol.22 , pp. 571-582
    • Bernath-Levin, K.1
  • 11
    • 0035845584 scopus 로고    scopus 로고
    • Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis
    • Jennings, C., West, J., Waine, C., Craik, D. & Anderson, M. Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. Proc. Natl Acad. Sci. USA 98, 10614-10619 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10614-10619
    • Jennings, C.1    West, J.2    Waine, C.3    Craik, D.4    Anderson, M.5
  • 12
    • 47849105966 scopus 로고    scopus 로고
    • Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata (golden apple snail )
    • Plan, M. R., Saska, I., Cagauan, A. G. & Craik, D. J. Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata (golden apple snail ). J. Agric. Food Chem. 56, 5237-5241 (2008).
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 5237-5241
    • Plan, M.R.1    Saska, I.2    Cagauan, A.G.3    Craik, D.J.4
  • 13
    • 43949110597 scopus 로고    scopus 로고
    • Cyclotides: Natural, circular plant peptides that possess significant activity against gastrointestinal nematode parasites of sheep
    • Colgrave, M. L. et al. Cyclotides: natural, circular plant peptides that possess significant activity against gastrointestinal nematode parasites of sheep. Biochemistry 47, 5581-5589 (2008).
    • (2008) Biochemistry , vol.47 , pp. 5581-5589
    • Colgrave, M.L.1
  • 14
    • 57849088141 scopus 로고    scopus 로고
    • Anthelmintic activity of cyclotides: In vitro studies with canine and human hookworms
    • Colgrave, M. L. et al. Anthelmintic activity of cyclotides: In vitro studies with canine and human hookworms. Acta Trop. 109, 163-166 (2009).
    • (2009) Acta Trop. , vol.109 , pp. 163-166
    • Colgrave, M.L.1
  • 15
    • 84879017232 scopus 로고    scopus 로고
    • Cyclotides as grafting frameworks for protein engineering and drug design applications
    • Poth, A. G., Chan, L. Y. & Craik, D. J. Cyclotides as grafting frameworks for protein engineering and drug design applications. Biopolymers 100, 480-491 (2013).
    • (2013) Biopolymers , vol.100 , pp. 480-491
    • Poth, A.G.1    Chan, L.Y.2    Craik, D.J.3
  • 16
    • 25444448796 scopus 로고    scopus 로고
    • Engineering stable peptide toxins by means of backbone cyclization: Stabilization of the alpha-conotoxin MII
    • Clark, R. J. et al. Engineering stable peptide toxins by means of backbone cyclization: stabilization of the alpha-conotoxin MII. Proc. Natl Acad. Sci. USA 102, 2-7 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2-7
    • Clark, R.J.1
  • 17
    • 77956502216 scopus 로고    scopus 로고
    • The engineering of an orally active conotoxin for the treatment of neuropathic pain
    • Clark, R. J. et al. The engineering of an orally active conotoxin for the treatment of neuropathic pain. Angew. Chem. Int. Ed. Engl. 49, 6545-6548 (2010).
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 6545-6548
    • Clark, R.J.1
  • 18
    • 84874966168 scopus 로고    scopus 로고
    • Cyclization of the antimicrobial peptide gomesin with native chemical ligation: Influences on stability and bioactivity
    • Chan, L. Y. et al. Cyclization of the antimicrobial peptide gomesin with native chemical ligation: influences on stability and bioactivity. Chembiochem 14, 617-624 (2013).
    • (2013) Chembiochem , vol.14 , pp. 617-624
    • Chan, L.Y.1
  • 19
    • 84857671453 scopus 로고    scopus 로고
    • Host-defense activities of cyclotides
    • Craik, D. J. Host-defense activities of cyclotides. Toxins (Basel) 4, 139-156 (2012).
    • (2012) Toxins (Basel) , vol.4 , pp. 139-156
    • Craik, D.J.1
  • 20
    • 84910617831 scopus 로고    scopus 로고
    • Backbone cyclization of a recombinant cystine-knot peptide by engineered sortase a
    • Stanger, K. et al. Backbone cyclization of a recombinant cystine-knot peptide by engineered Sortase A. FEBS Lett. 588, 4487-4496 (2014).
    • (2014) FEBS Lett. , vol.588 , pp. 4487-4496
    • Stanger, K.1
  • 21
    • 84864983594 scopus 로고    scopus 로고
    • Insights into processing and cyclization events associated with biosynthesis of the cyclic peptide kalata b1
    • Conlan, B. F. et al. Insights into processing and cyclization events associated with biosynthesis of the cyclic Peptide kalata B1. J. Biol. Chem. 287, 28037-28046 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 28037-28046
    • Conlan, B.F.1
  • 22
    • 79955058492 scopus 로고    scopus 로고
    • Albumins and their processing machinery are hijacked for cyclic peptides in sunflower
    • Mylne, J. S. et al. Albumins and their processing machinery are hijacked for cyclic peptides in sunflower. Nat. Chem. Biol. 7, 257-259 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 257-259
    • Mylne, J.S.1
  • 23
    • 0031259680 scopus 로고    scopus 로고
    • Expression and activation of the vacuolar processing enzyme in Saccharomyces cerevisiae
    • Hiraiwa, N., Nishimura, M. & Hara-Nishimura, I. Expression and activation of the vacuolar processing enzyme in Saccharomyces cerevisiae. Plant J. 12, 819-829 (1997).
    • (1997) Plant J. , vol.12 , pp. 819-829
    • Hiraiwa, N.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 24
    • 0032970657 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is self-catalytically activated by sequential removal of the c-terminal and n-terminal propeptides
    • Hiraiwa, N., Nishimura, M. & Hara-Nishimura, I. Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides. FEBS Lett. 447, 213-216 (1999).
    • (1999) FEBS Lett. , vol.447 , pp. 213-216
    • Hiraiwa, N.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 25
    • 0036005912 scopus 로고    scopus 로고
    • Activation of arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the c-terminal propeptide
    • Kuroyanagi, M. et al. Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide. Plant Cell Physiol. 43, 143-151 (2002).
    • (2002) Plant Cell Physiol. , vol.43 , pp. 143-151
    • Kuroyanagi, M.1
  • 26
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific flurometric assays
    • Kembhavi, A. A., Buttle, D. J., Knight, G. & Barrett, A. J. The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific flurometric assays. Arch. Biochem. Biophys. 303, 208-213 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, G.3    Barrett, A.J.4
  • 27
    • 3843128438 scopus 로고    scopus 로고
    • A plant vacuolar protease, VPE, mediates virus-induced hypersensitive cell death
    • Hatsugai, N. et al. A plant vacuolar protease, VPE, mediates virus-induced hypersensitive cell death. Science 305, 855-858 (2004).
    • (2004) Science , vol.305 , pp. 855-858
    • Hatsugai, N.1
  • 28
    • 84879731123 scopus 로고    scopus 로고
    • Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation
    • Dall, E. & Brandstetter, H. Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation. Proc. Natl Acad. Sci. USA 110, 10940-10945 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 10940-10945
    • Dall, E.1    Brandstetter, H.2
  • 29
    • 0030992979 scopus 로고    scopus 로고
    • Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase
    • Chen, J. et al. Cloning, Isolation, and Characterization of Mammalian Legumain, an Asparaginyl Endopeptidase. J. Biol. Chem. 272, 8090-8098 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 8090-8098
    • Chen, J.1
  • 30
    • 79955560420 scopus 로고    scopus 로고
    • Circular proteins and mechanisms of cyclization
    • Conlan, B. F. et al. Circular proteins and mechanisms of cyclization. Biopolymers 94, 573-583 (2010).
    • (2010) Biopolymers , vol.94 , pp. 573-583
    • Conlan, B.F.1
  • 31
    • 84923342100 scopus 로고    scopus 로고
    • Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain
    • Dall, E., Fegg, J. C., Briza, P. & Brandstetter, H. Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain. Angew. Chem. Int. Ed. Engl. 54, 2917-2921 (2015).
    • (2015) Angew. Chem. Int. Ed. Engl. , vol.54 , pp. 2917-2921
    • Dall, E.1    Fegg, J.C.2    Briza, P.3    Brandstetter, H.4
  • 32
    • 25444495498 scopus 로고    scopus 로고
    • Binding hot spot for invasion inhibitory molecules on plasmodium falciparum apical membrane antigen 1
    • Harris, K. S. et al. Binding hot spot for invasion inhibitory molecules on plasmodium falciparum apical membrane antigen 1. Infect. Immun. 73, 6981-6989 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 6981-6989
    • Harris, K.S.1
  • 33
    • 66149111751 scopus 로고    scopus 로고
    • Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning
    • Harris, K. S. et al. Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning. J. Biol. Chem. 284, 9361-9371 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 9361-9371
    • Harris, K.S.1
  • 34
    • 0027477474 scopus 로고
    • Asparaginyl endopeptidase of jack bean seeds
    • Abe, Y. et al. Asparaginyl Endopeptidase of Jack Bean Seeds. J. Biol. Chem. 268, 3525-3529 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 3525-3529
    • Abe, Y.1
  • 35
    • 84855998523 scopus 로고    scopus 로고
    • Activation of legumain involves proteolytic and conformational events, resulting in a context-and substrate-dependent activity profile
    • Dall, E. & Brandstetter, H. Activation of legumain involves proteolytic and conformational events, resulting in a context-and substrate-dependent activity profile. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 68, 24-31 (2012).
    • (2012) Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. , vol.68 , pp. 24-31
    • Dall, E.1    Brandstetter, H.2
  • 36
    • 0032189364 scopus 로고    scopus 로고
    • Cloning and expression of mouse legumain, a lysosomal endopeptidase
    • Chen, J. M., Dando, P. M., Stevens, R. A, Fortunato, M. & Barrett, A J. Cloning and expression of mouse legumain, a lysosomal endopeptidase. Biochem. J. 335(Pt 1): 111-117 (1998).
    • (1998) Biochem. J. , vol.335 , pp. 111-117
    • Chen, J.M.1    Dando, P.M.2    Stevens, R.A.3    Fortunato, M.4    Barrett, A.J.5
  • 37
    • 78149276862 scopus 로고    scopus 로고
    • Circular logic: Nonribosomal peptide-like macrocyclization with a ribosomal peptide catalyst
    • McIntosh, J. A. et al. Circular logic: nonribosomal peptide-like macrocyclization with a ribosomal peptide catalyst. J. Am. Chem. Soc. 132, 15499-15501 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15499-15501
    • McIntosh, J.A.1
  • 38
    • 84864709843 scopus 로고    scopus 로고
    • The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain
    • Koehnke, J., Bent, A., Houssen, W. E., Zollman, D. & Morawitz, F. The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain. Nat. Struct. Mol. Biol. 19, 767-772 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 767-772
    • Koehnke, J.1    Bent, A.2    Houssen, W.E.3    Zollman, D.4    Morawitz, F.5
  • 39
    • 3743136276 scopus 로고    scopus 로고
    • The role of proteolysis in the processing and assembly of 11S seed globulins
    • Jung, R. et al. The role of proteolysis in the processing and assembly of 11S seed globulins. Plant Cell 10, 343-357 (1998).
    • (1998) Plant Cell , vol.10 , pp. 343-357
    • Jung, R.1
  • 40
    • 8844279131 scopus 로고    scopus 로고
    • Capped acyclic permutants of the circular protein kalata B1
    • Simonsen, S. M., Daly, N. L. & Craik, D. J. Capped acyclic permutants of the circular protein kalata B1. FEBS Lett. 577, 399-402 (2004).
    • (2004) FEBS Lett. , vol.577 , pp. 399-402
    • Simonsen, S.M.1    Daly, N.L.2    Craik, D.J.3
  • 41
    • 84859768479 scopus 로고    scopus 로고
    • Oases: Robust de novo RNA-seq assembly across the dynamic range of expression levels
    • Schulz, M. H., Zerbino, D. R., Vingron, M. & Birney, E. Oases: robust de novo RNA-seq assembly across the dynamic range of expression levels. Bioinformatics 28, 1086-1092 (2012).
    • (2012) Bioinformatics , vol.28 , pp. 1086-1092
    • Schulz, M.H.1    Zerbino, D.R.2    Vingron, M.3    Birney, E.4
  • 42
    • 33745634395 scopus 로고    scopus 로고
    • Cd-hit: A fast program for clustering and comparing large sets of protein or nucleotide sequences
    • Li, W. & Godzik, A. Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 22, 1658-1659 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 1658-1659
    • Li, W.1    Godzik, A.2
  • 43
    • 67649884743 scopus 로고    scopus 로고
    • Fast and accurate short read alignment with Burrows-Wheeler transform
    • Li, H. & Durbin, R. Fast and accurate short read alignment with Burrows-Wheeler transform. Bioinformatics 25, 1754-1760 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 1754-1760
    • Li, H.1    Durbin, R.2
  • 44
    • 77949469889 scopus 로고    scopus 로고
    • Identification of candidates for cyclotide biosynthesis and cyclisation by expressed sequence tag analysis of Oldenlandia affinis
    • Qin, Q. et al. Identification of candidates for cyclotide biosynthesis and cyclisation by expressed sequence tag analysis of Oldenlandia affinis. BMC Genomics 11, 111 (2010).
    • (2010) BMC Genomics , vol.11 , pp. 111
    • Qin, Q.1
  • 46
    • 34447321852 scopus 로고    scopus 로고
    • Enhancements and modifications of primer design program Primer3
    • Koressaar, T. & Remm, M. Enhancements and modifications of primer design program Primer3. Bioinformatics 23, 1289-1291 (2007).
    • (2007) Bioinformatics , vol.23 , pp. 1289-1291
    • Koressaar, T.1    Remm, M.2
  • 47
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • Catanzariti, A., Soboleva, T. A., Jans, D. A., Board, P. G. & Baker, R. T. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13, 1331-1339 (2004).
    • (2004) Protein Sci. , vol.13 , pp. 1331-1339
    • Catanzariti, A.1    Soboleva, T.A.2    Jans, D.A.3    Board, P.G.4    Baker, R.T.5
  • 48
    • 0033557480 scopus 로고    scopus 로고
    • Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction
    • Liu, Y. et al. Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction. Anal. Biochem. 267, 331-335 (1999).
    • (1999) Anal. Biochem. , vol.267 , pp. 331-335
    • Liu, Y.1


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