메뉴 건너뛰기




Volumn 64, Issue 3, 2016, Pages 197-205

Rapid addition of unlabeled silent solubility tags to proteins using a new substrate-fused sortase reagent

Author keywords

Protein ligation; Silent solubility tag; Sortase; SUMO

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; NUCLEOPHILE; PHOP PROTEIN; POLYHISTIDINE TAG; POLYPEPTIDE; PROTEIN; PROTEIN TAG; REAGENT; SMALL UBIQUITIN LIKE MODIFIER PROTEIN; SORTASE; SORTASE A; UNCLASSIFIED DRUG; AMINOACYLTRANSFERASE; BACTERIAL PROTEIN; CYSTEINE PROTEINASE; SUMO 1 PROTEIN;

EID: 84957558018     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-016-0019-z     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 57149115773 scopus 로고    scopus 로고
    • Lipid modification of proteins through sortase-catalyzed transpeptidation
    • Antos JM, Miller GM, Grotenbreg GM, Ploegh HL (2008) Lipid modification of proteins through sortase-catalyzed transpeptidation. J Am Chem Soc 130:16338-16343. doi: 10.1021/ja806779e
    • (2008) J Am Chem Soc , vol.130 , pp. 16338-16343
    • Antos, J.M.1    Miller, G.M.2    Grotenbreg, G.M.3    Ploegh, H.L.4
  • 3
    • 43149108336 scopus 로고    scopus 로고
    • Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation
    • 10.1371/journal.pone.0001164 2007PLoSO.2.1164C
    • Chan L, Cross HF, She JK et al (2007) Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation. PLoS ONE 2:e1164. doi: 10.1371/journal.pone.0001164
    • (2007) PLoS ONE , vol.2 , pp. e1164
    • Chan, L.1    Cross, H.F.2    She, J.K.3
  • 4
    • 79960980943 scopus 로고    scopus 로고
    • A general strategy for the evolution of bond-forming enzymes using yeast display
    • 10.1073/pnas.1101046108 2011PNAS.10811399C
    • Chen I, Dorr BM, Liu DR (2011) A general strategy for the evolution of bond-forming enzymes using yeast display. Proc Natl Acad Sci USA 108:11399-11404. doi: 10.1073/pnas.1101046108
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11399-11404
    • Chen, I.1    Dorr, B.M.2    Liu, D.R.3
  • 5
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3
  • 6
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • di Guan C, Li P, Riggs PD, Inouye H (1988) Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67:21-30
    • (1988) Gene , vol.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 7
    • 84942366316 scopus 로고    scopus 로고
    • Efficient segmental isotope labeling of multi-domain proteins using Sortase A
    • 10.1007/s10858-015-9981-0
    • Freiburger L, Sonntag M, Hennig J et al (2015) Efficient segmental isotope labeling of multi-domain proteins using Sortase A. J Biomol NMR 63:1-8. doi: 10.1007/s10858-015-9981-0
    • (2015) J Biomol NMR , vol.63 , pp. 1-8
    • Freiburger, L.1    Sonntag, M.2    Hennig, J.3
  • 8
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • 10.1002/pro.5560061109
    • Huth JR, Bewley CA, Jackson BM et al (1997) Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci 6:2359-2364. doi: 10.1002/pro.5560061109
    • (1997) Protein Sci , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3
  • 9
    • 0035932982 scopus 로고    scopus 로고
    • Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus
    • 10.1073/pnas.101064198 2001PNAS.98.6056I
    • Ilangovan U, Ton-That H, Iwahara J et al (2001) Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proc Natl Acad Sci USA 98:6056-6061. doi: 10.1073/pnas.101064198
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6056-6061
    • Ilangovan, U.1    Ton-That, H.2    Iwahara, J.3
  • 10
    • 61549135769 scopus 로고    scopus 로고
    • Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method
    • 10.1007/s10858-008-9296-5
    • Kobashigawa Y, Kumeta H, Ogura K, Inagaki F (2009) Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method. J Biomol NMR 43:145-150. doi: 10.1007/s10858-008-9296-5
    • (2009) J Biomol NMR , vol.43 , pp. 145-150
    • Kobashigawa, Y.1    Kumeta, H.2    Ogura, K.3    Inagaki, F.4
  • 11
    • 33846809157 scopus 로고    scopus 로고
    • Dependence of effective molarity on linker length for an intramolecular protein-ligand system
    • 10.1021/ja066780e
    • Krishnamurthy VM, Semetey V, Bracher PJ et al (2007) Dependence of effective molarity on linker length for an intramolecular protein-ligand system. J Am Chem Soc 129:1312-1320. doi: 10.1021/ja066780e
    • (2007) J Am Chem Soc , vol.129 , pp. 1312-1320
    • Krishnamurthy, V.M.1    Semetey, V.2    Bracher, P.J.3
  • 12
    • 0011962568 scopus 로고    scopus 로고
    • Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
    • LaVallie ER, Lu Z, Diblasio-Smith EA et al (2000) Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli. Methods Enzymol 326:322-340
    • (2000) Methods Enzymol , vol.326 , pp. 322-340
    • LaVallie, E.R.1    Lu, Z.2    Diblasio-Smith, E.A.3
  • 13
    • 79953733187 scopus 로고    scopus 로고
    • Protein-protein fusion catalyzed by sortase A
    • 10.1371/journal.pone.0018342 2011PLoSO.618342L
    • Levary DA, Parthasarathy R, Boder ET, Ackerman ME (2011) Protein-protein fusion catalyzed by sortase A. PLoS ONE 6:e18342. doi: 10.1371/journal.pone.0018342
    • (2011) PLoS ONE , vol.6 , pp. e18342
    • Levary, D.A.1    Parthasarathy, R.2    Boder, E.T.3    Ackerman, M.E.4
  • 14
    • 84942501319 scopus 로고    scopus 로고
    • Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis
    • 10.1007/s10858-015-9965-0
    • Macdonald R, Sarkar D, Amer BR, Clubb RT (2015) Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis. J Biomol NMR 63:111-117. doi: 10.1007/s10858-015-9965-0
    • (2015) J Biomol NMR , vol.63 , pp. 111-117
    • MacDonald, R.1    Sarkar, D.2    Amer, B.R.3    Clubb, R.T.4
  • 15
    • 3543073550 scopus 로고    scopus 로고
    • SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins
    • 10.1023/B:JSFG.0000029237.70316.52
    • Malakhov MP, Mattern MR, Malakhova OA et al (2004) SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins. J Struct Funct Genomics 5:75-86. doi: 10.1023/B:JSFG.0000029237.70316.52
    • (2004) J Struct Funct Genomics , vol.5 , pp. 75-86
    • Malakhov, M.P.1    Mattern, M.R.2    Malakhova, O.A.3
  • 16
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO
    • 10.1110/ps.051812706
    • Marblestone JG, Edavettal SC, Lim Y et al (2006) Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO. Protein Sci 15:182-189. doi: 10.1110/ps.051812706
    • (2006) Protein Sci , vol.15 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3
  • 17
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • 10.1126/science.285.5428.760
    • Mazmanian SK (1999) Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285:760-763. doi: 10.1126/science.285.5428.760
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1
  • 18
    • 77749324909 scopus 로고    scopus 로고
    • Segmental isotopic labeling of multi-domain and fusion proteins by protein trans-splicing in vivo and in vitro
    • 10.1038/nprot.2009.240
    • Muona M, Aranko AS, Raulinaitis V, Iwaï H (2010) Segmental isotopic labeling of multi-domain and fusion proteins by protein trans-splicing in vivo and in vitro. Nat Protoc 5:574-587. doi: 10.1038/nprot.2009.240
    • (2010) Nat Protoc , vol.5 , pp. 574-587
    • Muona, M.1    Aranko, A.S.2    Raulinaitis, V.3    Iwaï, H.4
  • 19
    • 33644984956 scopus 로고    scopus 로고
    • Staphylococcus aureus Sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop
    • 10.1074/jbc.M506123200
    • Naik MT, Suree N, Ilangovan U et al (2006) Staphylococcus aureus Sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop. J Biol Chem 281:1817-1826. doi: 10.1074/jbc.M506123200
    • (2006) J Biol Chem , vol.281 , pp. 1817-1826
    • Naik, M.T.1    Suree, N.2    Ilangovan, U.3
  • 20
    • 59249094982 scopus 로고    scopus 로고
    • SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems
    • Panavas T, Sanders C, Butt TR (2009) SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems. Methods Mol Biol 497:303-317. doi: 10.1007/978-1-59745-566-4-20
    • (2009) Methods Mol Biol , vol.497 , pp. 303-317
    • Panavas, T.1    Sanders, C.2    Butt, T.R.3
  • 21
    • 33947664974 scopus 로고    scopus 로고
    • Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation
    • 10.1021/bc060339w
    • Parthasarathy R, Subramanian S, Boder ET (2007) Sortase A as a novel molecular "stapler" for sequence-specific protein conjugation. Bioconjug Chem 18:469-476. doi: 10.1021/bc060339w
    • (2007) Bioconjug Chem , vol.18 , pp. 469-476
    • Parthasarathy, R.1    Subramanian, S.2    Boder, E.T.3
  • 22
    • 78049401859 scopus 로고    scopus 로고
    • Domain structure of virulence-associated response regulator PhoP of Mycobacterium tuberculosis: Role of the linker region in regulator-promoter interaction(s)
    • 10.1074/jbc.M110.135822
    • Pathak A, Goyal R, Sinha A, Sarkar D (2010) Domain structure of virulence-associated response regulator PhoP of Mycobacterium tuberculosis: role of the linker region in regulator-promoter interaction(s). J Biol Chem 285:34309-34318. doi: 10.1074/jbc.M110.135822
    • (2010) J Biol Chem , vol.285 , pp. 34309-34318
    • Pathak, A.1    Goyal, R.2    Sinha, A.3    Sarkar, D.4
  • 23
    • 79952459386 scopus 로고    scopus 로고
    • SUMO fusion technology for enhanced protein expression and purification in prokaryotes and eukaryotes
    • Peroutka Iii RJ, Orcutt SJ, Strickler JE, Butt TR (2011) SUMO fusion technology for enhanced protein expression and purification in prokaryotes and eukaryotes. Methods Mol Biol 705:15-30. doi: 10.1007/978-1-61737-967-3-2
    • (2011) Methods Mol Biol , vol.705 , pp. 15-30
    • Peroutka, R.J.1    Orcutt, S.J.2    Strickler, J.E.3    Butt, T.R.4
  • 24
    • 0037013286 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring
    • 10.1074/jbc.M109194200
    • Perry AM, Ton-That H, Mazmanian SK, Schneewind O (2002) Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring. J Biol Chem 277:16241-16248. doi: 10.1074/jbc.M109194200
    • (2002) J Biol Chem , vol.277 , pp. 16241-16248
    • Perry, A.M.1    Ton-That, H.2    Mazmanian, S.K.3    Schneewind, O.4
  • 25
    • 34248575231 scopus 로고    scopus 로고
    • Synthesis of biologically active peptide nucleic acid-peptide conjugates by sortase-mediated ligation
    • 10.1021/jo062331l
    • Pritz S, Wolf Y, Kraetke O et al (2007) Synthesis of biologically active peptide nucleic acid-peptide conjugates by sortase-mediated ligation. J Org Chem 72:3909-3912. doi: 10.1021/jo062331l
    • (2007) J Org Chem , vol.72 , pp. 3909-3912
    • Pritz, S.1    Wolf, Y.2    Kraetke, O.3
  • 26
    • 79951556764 scopus 로고    scopus 로고
    • Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
    • 10.1007/s10858-010-9464-2
    • Refaei MA, Combs A, Kojetin DJ et al (2011) Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy. J Biomol NMR 49:3-7. doi: 10.1007/s10858-010-9464-2
    • (2011) J Biomol NMR , vol.49 , pp. 3-7
    • Refaei, M.A.1    Combs, A.2    Kojetin, D.J.3
  • 27
    • 78650363751 scopus 로고    scopus 로고
    • Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker
    • 10.1021/bc100206z
    • Sakamoto T, Sawamoto S, Tanaka T et al (2010) Enzyme-mediated site-specific antibody-protein modification using a ZZ domain as a linker. Bioconjug Chem 21:2227-2233. doi: 10.1021/bc100206z
    • (2010) Bioconjug Chem , vol.21 , pp. 2227-2233
    • Sakamoto, T.1    Sawamoto, S.2    Tanaka, T.3
  • 28
    • 84902264443 scopus 로고    scopus 로고
    • Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteria
    • 10.1016/j.bbamcr.2013.11.009
    • Schneewind O, Missiakas D (2014) Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteria. Biochim Biophys Acta 1843:1687-1697. doi: 10.1016/j.bbamcr.2013.11.009
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 1687-1697
    • Schneewind, O.1    Missiakas, D.2
  • 29
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson KS (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 30
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • 10.1111/j.1365-2958.2011.07887.x
    • Spirig T, Weiner EM, Clubb RT (2011) Sortase enzymes in Gram-positive bacteria. Mol Microbiol 82:1044-1059. doi: 10.1111/j.1365-2958.2011.07887.x
    • (2011) Mol Microbiol , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 31
    • 0033582287 scopus 로고    scopus 로고
    • Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
    • 10.1073/pnas.96.2.388 1999PNAS.96.388X
    • Xu R, Ayers B, Cowburn D, Muir TW (1999) Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc Natl Acad Sci 96:388-393. doi: 10.1073/pnas.96.2.388
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 388-393
    • Xu, R.1    Ayers, B.2    Cowburn, D.3    Muir, T.W.4
  • 32
    • 0032503612 scopus 로고    scopus 로고
    • Segmental isotope labeling for protein NMR using peptide splicing
    • 10.1021/ja980776o
    • Yamazaki T, Otomo T, Oda N et al (1998) Segmental isotope labeling for protein NMR using peptide splicing. J Am Chem Soc 120:5591-5592. doi: 10.1021/ja980776o
    • (1998) J Am Chem Soc , vol.120 , pp. 5591-5592
    • Yamazaki, T.1    Otomo, T.2    Oda, N.3
  • 33
    • 77649176543 scopus 로고    scopus 로고
    • Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies
    • 10.1007/s10858-009-9371-6
    • Zhou P, Wagner G (2009) Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies. J Biomol NMR 46:23-31. doi: 10.1007/s10858-009-9371-6
    • (2009) J Biomol NMR , vol.46 , pp. 23-31
    • Zhou, P.1    Wagner, G.2
  • 34
    • 0034987544 scopus 로고    scopus 로고
    • A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins
    • Zhou P, Lugovskoy AA, Wagner G (2001) A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins. J Biomol NMR 20:11-14
    • (2001) J Biomol NMR , vol.20 , pp. 11-14
    • Zhou, P.1    Lugovskoy, A.A.2    Wagner, G.3
  • 35
    • 24944448735 scopus 로고    scopus 로고
    • Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies
    • 10.1038/nbt1097
    • Züger S, Iwai H (2005) Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies. Nat Biotechnol 23:736-740. doi: 10.1038/nbt1097
    • (2005) Nat Biotechnol , vol.23 , pp. 736-740
    • Züger, S.1    Iwai, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.