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Volumn 52, Issue 34, 2013, Pages 5920-5927

Internal disulfide bond acts as a switch for intein activity

Author keywords

[No Author keywords available]

Indexed keywords

CYS RESIDUES; DIFFERENTIAL ACTIVITY; DISULFIDE BONDS; DNA POLYMERASE; E. COLI; OVER-EXPRESSION; PHYSIOLOGICAL ROLES; PROTEIN-SPLICING;

EID: 84883228193     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400736c     Document Type: Article
Times cited : (27)

References (61)
  • 1
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H. (2000) Protein splicing and related forms of protein autoprocessing Annu. Rev. Biochem. 69, 447-496
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 2
    • 84876461880 scopus 로고    scopus 로고
    • Recent progress in intein research: From mechanism to directed evolution and applications
    • Volkmann, G. and Mootz, H. D. (2013) Recent progress in intein research: from mechanism to directed evolution and applications Cell. Mol. Life Sci. 70, 1185-1206
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1185-1206
    • Volkmann, G.1    Mootz, H.D.2
  • 3
    • 0026774103 scopus 로고
    • Protein splicing in the maturation of M. Tuberculosis recA protein: A mechanism for tolerating a novel class of intervening sequence
    • Davis, E. O., Jenner, P. J., Brooks, P. C., Colston, M. J., and Sedgwick, S. G. (1992) Protein splicing in the maturation of M. tuberculosis recA protein: a mechanism for tolerating a novel class of intervening sequence Cell 71, 201-210
    • (1992) Cell , vol.71 , pp. 201-210
    • Davis, E.O.1    Jenner, P.J.2    Brooks, P.C.3    Colston, M.J.4    Sedgwick, S.G.5
  • 4
    • 0030952831 scopus 로고    scopus 로고
    • Identification of three core regions essential for protein splicing of the yeast Vma1 Protozyme. A random mutagenesis study of the entire Vma1-derived endonuclease sequence
    • Kawasaki, M., Nogami, S., Satow, Y., Ohya, Y., and Anraku, Y. (1997) Identification of three core regions essential for protein splicing of the yeast Vma1 Protozyme. A random mutagenesis study of the entire Vma1-derived endonuclease sequence J. Biol. Chem. 272, 15668-15674
    • (1997) J. Biol. Chem. , vol.272 , pp. 15668-15674
    • Kawasaki, M.1    Nogami, S.2    Satow, Y.3    Ohya, Y.4    Anraku, Y.5
  • 5
    • 33751233858 scopus 로고    scopus 로고
    • Inteins, introns, and homing endonucleases: Recent revelations about the life cycle of parasitic genetic elements
    • Gogarten, J. P. and Hilario, E. (2006) Inteins, introns, and homing endonucleases: recent revelations about the life cycle of parasitic genetic elements BMC Evol. Biol. 6, 94
    • (2006) BMC Evol. Biol. , vol.6 , pp. 94
    • Gogarten, J.P.1    Hilario, E.2
  • 7
    • 0035425040 scopus 로고    scopus 로고
    • Intein spread and extinction in evolution
    • Pietrokovski, S. (2001) Intein spread and extinction in evolution Trends Genet. 17, 465-472
    • (2001) Trends Genet. , vol.17 , pp. 465-472
    • Pietrokovski, S.1
  • 8
    • 76049084239 scopus 로고    scopus 로고
    • Conservation of intron and intein insertion sites: Implications for life histories of parasitic genetic elements
    • Swithers, K. S., Senejani, A. G., Fournier, G. P., and Gogarten, J. P. (2009) Conservation of intron and intein insertion sites: implications for life histories of parasitic genetic elements BMC Evol. Biol. 9, 303
    • (2009) BMC Evol. Biol. , vol.9 , pp. 303
    • Swithers, K.S.1    Senejani, A.G.2    Fournier, G.P.3    Gogarten, J.P.4
  • 10
    • 32044468517 scopus 로고    scopus 로고
    • Protein trans-splicing and characterization of a split family B-type DNA polymerase from the hyperthermophilic archaeal parasite Nanoarchaeum equitans
    • Choi, J. J., Nam, K. H., Min, B., Kim, S. J., Soll, D., and Kwon, S. T. (2006) Protein trans-splicing and characterization of a split family B-type DNA polymerase from the hyperthermophilic archaeal parasite Nanoarchaeum equitans J. Mol. Biol. 356, 1093-1106
    • (2006) J. Mol. Biol. , vol.356 , pp. 1093-1106
    • Choi, J.J.1    Nam, K.H.2    Min, B.3    Kim, S.J.4    Soll, D.5    Kwon, S.T.6
  • 11
    • 2442718804 scopus 로고    scopus 로고
    • Protein splicing of a Pyrococcus abyssi intein with a C-terminal glutamine
    • Mills, K. V., Manning, J. S., Garcia, A. M., and Wuerdeman, L. A. (2004) Protein splicing of a Pyrococcus abyssi intein with a C-terminal glutamine J. Biol. Chem. 279, 20685-20691
    • (2004) J. Biol. Chem. , vol.279 , pp. 20685-20691
    • Mills, K.V.1    Manning, J.S.2    Garcia, A.M.3    Wuerdeman, L.A.4
  • 12
    • 77954377503 scopus 로고    scopus 로고
    • Photomodulation of protein trans-splicing through backbone photocaging of the DnaE split intein
    • Berrade, L., Kwon, Y., and Camarero, J. A. (2010) Photomodulation of protein trans-splicing through backbone photocaging of the DnaE split intein ChemBioChem 11, 1368-1372
    • (2010) ChemBioChem , vol.11 , pp. 1368-1372
    • Berrade, L.1    Kwon, Y.2    Camarero, J.A.3
  • 13
    • 54749102251 scopus 로고    scopus 로고
    • Activation of protein splicing by protease- or light-triggered O to N acyl migration
    • Vila-Perello, M., Hori, Y., Ribo, M., and Muir, T. W. (2008) Activation of protein splicing by protease- or light-triggered O to N acyl migration Angew. Chem., Int. Ed. Engl. 47, 7764-7767
    • (2008) Angew. Chem., Int. Ed. Engl. , vol.47 , pp. 7764-7767
    • Vila-Perello, M.1    Hori, Y.2    Ribo, M.3    Muir, T.W.4
  • 14
    • 79957473350 scopus 로고    scopus 로고
    • Directed evolution of a small-molecule-triggered intein with improved splicing properties in mammalian cells
    • Peck, S. H., Chen, I., and Liu, D. R. (2011) Directed evolution of a small-molecule-triggered intein with improved splicing properties in mammalian cells Chem. Biol. 18, 619-630
    • (2011) Chem. Biol. , vol.18 , pp. 619-630
    • Peck, S.H.1    Chen, I.2    Liu, D.R.3
  • 15
    • 13244252218 scopus 로고    scopus 로고
    • Regulation of protein activity with small-molecule-controlled inteins
    • Skretas, G. and Wood, D. W. (2005) Regulation of protein activity with small-molecule-controlled inteins Protein Sci. 14, 523-532
    • (2005) Protein Sci. , vol.14 , pp. 523-532
    • Skretas, G.1    Wood, D.W.2
  • 16
    • 78651401666 scopus 로고    scopus 로고
    • Cisplatin inhibits protein splicing, suggesting inteins as therapeutic targets in mycobacteria
    • Zhang, L., Zheng, Y., Callahan, B., Belfort, M., and Liu, Y. (2011) Cisplatin inhibits protein splicing, suggesting inteins as therapeutic targets in mycobacteria J. Biol. Chem. 286, 1277-1282
    • (2011) J. Biol. Chem. , vol.286 , pp. 1277-1282
    • Zhang, L.1    Zheng, Y.2    Callahan, B.3    Belfort, M.4    Liu, Y.5
  • 17
    • 0034518359 scopus 로고    scopus 로고
    • Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor
    • Wood, D. W., Derbyshire, V., Wu, W., Chartrain, M., Belfort, M., and Belfort, G. (2000) Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor Biotechnol. Prog. 16, 1055-1063
    • (2000) Biotechnol. Prog. , vol.16 , pp. 1055-1063
    • Wood, D.W.1    Derbyshire, V.2    Wu, W.3    Chartrain, M.4    Belfort, M.5    Belfort, G.6
  • 18
    • 0032832776 scopus 로고    scopus 로고
    • A genetic system yields self-cleaving inteins for bioseparations
    • Wood, D. W., Wu, W., Belfort, G., Derbyshire, V., and Belfort, M. (1999) A genetic system yields self-cleaving inteins for bioseparations Nat. Biotechnol. 17, 889-892
    • (1999) Nat. Biotechnol. , vol.17 , pp. 889-892
    • Wood, D.W.1    Wu, W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 19
    • 0036753960 scopus 로고    scopus 로고
    • Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli DNA gyrase subunit A
    • Adam, E. and Perler, F. B. (2002) Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli DNA gyrase subunit A J. Mol. Microbiol. Biotechnol. 4, 479-487
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 479-487
    • Adam, E.1    Perler, F.B.2
  • 20
    • 2442655671 scopus 로고    scopus 로고
    • Bacteriophage-based genetic system for selection of nonsplicing inteins
    • Cann, I. K., Amaya, K. R., Southworth, M. W., and Perler, F. B. (2004) Bacteriophage-based genetic system for selection of nonsplicing inteins Appl. Environ. Microbiol. 70, 3158-3162
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3158-3162
    • Cann, I.K.1    Amaya, K.R.2    Southworth, M.W.3    Perler, F.B.4
  • 21
    • 70350161834 scopus 로고    scopus 로고
    • Temperature-sensitive mutations made easy: Generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges
    • Tan, G., Chen, M., Foote, C., and Tan, C. (2009) Temperature-sensitive mutations made easy: generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges Genetics 183, 13-22
    • (2009) Genetics , vol.183 , pp. 13-22
    • Tan, G.1    Chen, M.2    Foote, C.3    Tan, C.4
  • 23
    • 79953009773 scopus 로고    scopus 로고
    • Photocontrol of protein activity mediated by the cleavage reaction of a split intein
    • Binschik, J., Zettler, J., and Mootz, H. D. (2011) Photocontrol of protein activity mediated by the cleavage reaction of a split intein Angew. Chem., Int. Ed. Engl. 50, 3249-3252
    • (2011) Angew. Chem., Int. Ed. Engl. , vol.50 , pp. 3249-3252
    • Binschik, J.1    Zettler, J.2    Mootz, H.D.3
  • 24
    • 3242694003 scopus 로고    scopus 로고
    • Directed evolution of ligand dependence: Small-molecule-activated protein splicing
    • Buskirk, A. R., Ong, Y. C., Gartner, Z. J., and Liu, D. R. (2004) Directed evolution of ligand dependence: small-molecule-activated protein splicing Proc. Natl. Acad. Sci. U. S. A. 101, 10505-10510
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10505-10510
    • Buskirk, A.R.1    Ong, Y.C.2    Gartner, Z.J.3    Liu, D.R.4
  • 25
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: A new tool to control protein structure and function in vitro and in vivo
    • Mootz, H. D., Blum, E. S., Tyszkiewicz, A. B., and Muir, T. W. (2003) Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo J. Am. Chem. Soc. 125, 10561-10569
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10561-10569
    • Mootz, H.D.1    Blum, E.S.2    Tyszkiewicz, A.B.3    Muir, T.W.4
  • 26
    • 0037036791 scopus 로고    scopus 로고
    • Protein splicing triggered by a small molecule
    • Mootz, H. D. and Muir, T. W. (2002) Protein splicing triggered by a small molecule J. Am. Chem. Soc. 124, 9044-9045
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9044-9045
    • Mootz, H.D.1    Muir, T.W.2
  • 27
    • 41449091908 scopus 로고    scopus 로고
    • Activation of protein splicing with light in yeast
    • Tyszkiewicz, A. B. and Muir, T. W. (2008) Activation of protein splicing with light in yeast Nat. Methods 5, 303-305
    • (2008) Nat. Methods , vol.5 , pp. 303-305
    • Tyszkiewicz, A.B.1    Muir, T.W.2
  • 28
    • 33745968727 scopus 로고    scopus 로고
    • Control of transcription factor activity and osteoblast differentiation in mammalian cells using an evolved small-molecule-dependent intein
    • Yuen, C. M., Rodda, S. J., Vokes, S. A., McMahon, A. P., and Liu, D. R. (2006) Control of transcription factor activity and osteoblast differentiation in mammalian cells using an evolved small-molecule-dependent intein J. Am. Chem. Soc. 128, 8939-8946
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8939-8946
    • Yuen, C.M.1    Rodda, S.J.2    Vokes, S.A.3    McMahon, A.P.4    Liu, D.R.5
  • 29
  • 30
    • 79955619798 scopus 로고    scopus 로고
    • Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
    • Callahan, B. P., Topilina, N. I., Stanger, M. J., Van Roey, P., and Belfort, M. (2011) Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications Nat. Struct. Mol. Biol. 18, 630-633
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 630-633
    • Callahan, B.P.1    Topilina, N.I.2    Stanger, M.J.3    Van Roey, P.4    Belfort, M.5
  • 31
    • 33750492267 scopus 로고    scopus 로고
    • Elimination of in vivo cleavage between target protein and intein in the intein-mediated protein purification systems
    • Cui, C., Zhao, W., Chen, J., Wang, J., and Li, Q. (2006) Elimination of in vivo cleavage between target protein and intein in the intein-mediated protein purification systems Protein Expression Purif. 50, 74-81
    • (2006) Protein Expression Purif. , vol.50 , pp. 74-81
    • Cui, C.1    Zhao, W.2    Chen, J.3    Wang, J.4    Li, Q.5
  • 32
    • 82955169570 scopus 로고    scopus 로고
    • Branched intermediate formation is the slowest step in the protein splicing reaction of the Ala1 KlbA intein from Methanococcus jannaschii
    • Saleh, L., Southworth, M. W., Considine, N., O'Neill, C., Benner, J., Bollinger, J. M., Jr., and Perler, F. B. (2011) Branched intermediate formation is the slowest step in the protein splicing reaction of the Ala1 KlbA intein from Methanococcus jannaschii Biochemistry 50, 10576-10589
    • (2011) Biochemistry , vol.50 , pp. 10576-10589
    • Saleh, L.1    Southworth, M.W.2    Considine, N.3    O'Neill, C.4    Benner, J.5    Bollinger, Jr.J.M.6    Perler, F.B.7
  • 33
    • 18244394306 scopus 로고    scopus 로고
    • Development of a tandem protein trans-splicing system based on native and engineered split inteins
    • Shi, J. and Muir, T. W. (2005) Development of a tandem protein trans-splicing system based on native and engineered split inteins J. Am. Chem. Soc. 127, 6198-6206
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6198-6206
    • Shi, J.1    Muir, T.W.2
  • 35
    • 0032584098 scopus 로고    scopus 로고
    • Protein splicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein
    • Mills, K. V., Lew, B. M., Jiang, S., and Paulus, H. (1998) Protein splicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein Proc. Natl. Acad. Sci. U. S. A. 95, 3543-3548
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3543-3548
    • Mills, K.V.1    Lew, B.M.2    Jiang, S.3    Paulus, H.4
  • 37
    • 0033963173 scopus 로고    scopus 로고
    • InBase, the Intein Database
    • Perler, F. B. (2000) InBase, the Intein Database Nucleic Acids Res. 28, 344-345
    • (2000) Nucleic Acids Res. , vol.28 , pp. 344-345
    • Perler, F.B.1
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 13244292480 scopus 로고    scopus 로고
    • Kinetic analysis of the individual steps of protein splicing for the Pyrococcus abyssi PolII intein
    • Mills, K. V., Dorval, D. M., and Lewandowski, K. T. (2005) Kinetic analysis of the individual steps of protein splicing for the Pyrococcus abyssi PolII intein J. Biol. Chem. 280, 2714-2720
    • (2005) J. Biol. Chem. , vol.280 , pp. 2714-2720
    • Mills, K.V.1    Dorval, D.M.2    Lewandowski, K.T.3
  • 42
    • 0034617214 scopus 로고    scopus 로고
    • Protein splicing in the absence of an intein penultimate histidine
    • Chen, L., Benner, J., and Perler, F. B. (2000) Protein splicing in the absence of an intein penultimate histidine J. Biol. Chem. 275, 20431-20435
    • (2000) J. Biol. Chem. , vol.275 , pp. 20431-20435
    • Chen, L.1    Benner, J.2    Perler, F.B.3
  • 43
    • 0036295886 scopus 로고    scopus 로고
    • Protein-splicing reaction via a thiazolidine intermediate: Crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides
    • Mizutani, R., Nogami, S., Kawasaki, M., Ohya, Y., Anraku, Y., and Satow, Y. (2002) Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides J. Mol. Biol. 316, 919-929
    • (2002) J. Mol. Biol. , vol.316 , pp. 919-929
    • Mizutani, R.1    Nogami, S.2    Kawasaki, M.3    Ohya, Y.4    Anraku, Y.5    Satow, Y.6
  • 44
    • 0030959311 scopus 로고    scopus 로고
    • Identification of an unusual intein in chloroplast ClpP protease of Chlamydomonas eugametos
    • Wang, S. and Liu, X. Q. (1997) Identification of an unusual intein in chloroplast ClpP protease of Chlamydomonas eugametos J. Biol. Chem. 272, 11869-11873
    • (1997) J. Biol. Chem. , vol.272 , pp. 11869-11873
    • Wang, S.1    Liu, X.Q.2
  • 45
    • 0036843028 scopus 로고    scopus 로고
    • Protein splicing of the Deinococcus radiodurans strain R1 Snf2 intein
    • Southworth, M. W. and Perler, F. B. (2002) Protein splicing of the Deinococcus radiodurans strain R1 Snf2 intein J. Bacteriol. 184, 6387-6388
    • (2002) J. Bacteriol. , vol.184 , pp. 6387-6388
    • Southworth, M.W.1    Perler, F.B.2
  • 46
    • 0032483013 scopus 로고    scopus 로고
    • Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocystis sp. PCC6803
    • Wu, H., Hu, Z., and Liu, X. Q. (1998) Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocystis sp. PCC6803 Proc. Natl. Acad. Sci. U. S. A. 95, 9226-9231
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9226-9231
    • Wu, H.1    Hu, Z.2    Liu, X.Q.3
  • 47
    • 77955120112 scopus 로고    scopus 로고
    • The Deinococcus radiodurans Snf2 intein caught in the act: Detection of the Class 3 intein signature Block F branched intermediate
    • Brace, L. E., Southworth, M. W., Tori, K., Cushing, M. L., and Perler, F. (2010) The Deinococcus radiodurans Snf2 intein caught in the act: detection of the Class 3 intein signature Block F branched intermediate Protein Sci. 19, 1525-1533
    • (2010) Protein Sci. , vol.19 , pp. 1525-1533
    • Brace, L.E.1    Southworth, M.W.2    Tori, K.3    Cushing, M.L.4    Perler, F.5
  • 48
    • 77249097494 scopus 로고    scopus 로고
    • Splicing of the mycobacteriophage Bethlehem DnaB intein: Identification of a new mechanistic class of inteins that contain an obligate block F nucleophile
    • Tori, K., Dassa, B., Johnson, M. A., Southworth, M. W., Brace, L. E., Ishino, Y., Pietrokovski, S., and Perler, F. B. (2010) Splicing of the mycobacteriophage Bethlehem DnaB intein: identification of a new mechanistic class of inteins that contain an obligate block F nucleophile J. Biol. Chem. 285, 2515-2526
    • (2010) J. Biol. Chem. , vol.285 , pp. 2515-2526
    • Tori, K.1    Dassa, B.2    Johnson, M.A.3    Southworth, M.W.4    Brace, L.E.5    Ishino, Y.6    Pietrokovski, S.7    Perler, F.B.8
  • 49
    • 79955387027 scopus 로고    scopus 로고
    • Expanding the definition of class 3 inteins and their proposed phage origin
    • Tori, K. and Perler, F. B. (2011) Expanding the definition of class 3 inteins and their proposed phage origin J. Bacteriol. 193, 2035-2041
    • (2011) J. Bacteriol. , vol.193 , pp. 2035-2041
    • Tori, K.1    Perler, F.B.2
  • 51
    • 77953806959 scopus 로고    scopus 로고
    • Branched intermediate formation stimulates peptide bond cleavage in protein splicing
    • Frutos, S., Goger, M., Giovani, B., Cowburn, D., and Muir, T. W. (2010) Branched intermediate formation stimulates peptide bond cleavage in protein splicing Nat. Chem. Biol. 6, 527-533
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 527-533
    • Frutos, S.1    Goger, M.2    Giovani, B.3    Cowburn, D.4    Muir, T.W.5
  • 52
    • 79551681995 scopus 로고    scopus 로고
    • Spontaneous proton transfer to a conserved intein residue determines on-pathway protein splicing
    • Pereira, B., Shemella, P. T., Amitai, G., Belfort, G., Nayak, S. K., and Belfort, M. (2011) Spontaneous proton transfer to a conserved intein residue determines on-pathway protein splicing J. Mol. Biol. 406, 430-442
    • (2011) J. Mol. Biol. , vol.406 , pp. 430-442
    • Pereira, B.1    Shemella, P.T.2    Amitai, G.3    Belfort, G.4    Nayak, S.K.5    Belfort, M.6
  • 53
    • 33847071304 scopus 로고    scopus 로고
    • Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue
    • Van Roey, P., Pereira, B., Li, Z., Hiraga, K., Belfort, M., and Derbyshire, V. (2007) Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue J. Mol. Biol. 367, 162-173
    • (2007) J. Mol. Biol. , vol.367 , pp. 162-173
    • Van Roey, P.1    Pereira, B.2    Li, Z.3    Hiraga, K.4    Belfort, M.5    Derbyshire, V.6
  • 54
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The Intein Database
    • Perler, F. B. (2002) InBase: the Intein Database Nucleic Acids Res. 30, 383-384
    • (2002) Nucleic Acids Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 55
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette, P. H., Aslund, F., Beckwith, J., and Georgiou, G. (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm Proc. Natl. Acad. Sci. U. S. A. 96, 13703-13708
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 56
    • 0002171638 scopus 로고
    • Methanogenus, a new genus of marin methanogenic bacteria, and characterization of Methanogenium cariaci sp. Nov. And Methanogenium marisnigri sp. nov
    • Romesser, J. A., Wolfe, R. S., Nayer, F., Speiss, E., and Walther-Mauruschat, A. (1979) Methanogenus, a new genus of marin methanogenic bacteria, and characterization of Methanogenium cariaci sp. nov. and Methanogenium marisnigri sp. nov Arch. Microbiol. 121, 147-153
    • (1979) Arch. Microbiol. , vol.121 , pp. 147-153
    • Romesser, J.A.1    Wolfe, R.S.2    Nayer, F.3    Speiss, E.4    Walther-Mauruschat, A.5
  • 57
    • 0035968177 scopus 로고    scopus 로고
    • Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein
    • Ghosh, I., Sun, L., and Xu, M. Q. (2001) Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein J. Biol. Chem. 276, 24051-24058
    • (2001) J. Biol. Chem. , vol.276 , pp. 24051-24058
    • Ghosh, I.1    Sun, L.2    Xu, M.Q.3
  • 58
    • 0035815658 scopus 로고    scopus 로고
    • Reversible inhibition of protein splicing by zinc ion
    • Mills, K. V. and Paulus, H. (2001) Reversible inhibition of protein splicing by zinc ion J. Biol. Chem. 276, 10832-10838
    • (2001) J. Biol. Chem. , vol.276 , pp. 10832-10838
    • Mills, K.V.1    Paulus, H.2
  • 59
    • 0037881919 scopus 로고    scopus 로고
    • Zinc ion effects on individual Ssp DnaE intein splicing steps: Regulating pathway progression
    • Nichols, N. M., Benner, J. S., Martin, D. D., and Evans, T. C., Jr. (2003) Zinc ion effects on individual Ssp DnaE intein splicing steps: regulating pathway progression Biochemistry 42, 5301-5311
    • (2003) Biochemistry , vol.42 , pp. 5301-5311
    • Nichols, N.M.1    Benner, J.S.2    Martin, D.D.3    Evans, Jr.T.C.4
  • 60
    • 27144547019 scopus 로고    scopus 로고
    • Crystal structures of an intein from the split dnaE gene of Synechocystis sp. PCC6803 reveal the catalytic model without the penultimate histidine and the mechanism of zinc ion inhibition of protein splicing
    • Sun, P., Ye, S., Ferrandon, S., Evans, T. C., Xu, M. Q., and Rao, Z. (2005) Crystal structures of an intein from the split dnaE gene of Synechocystis sp. PCC6803 reveal the catalytic model without the penultimate histidine and the mechanism of zinc ion inhibition of protein splicing J. Mol. Biol. 353, 1093-1105
    • (2005) J. Mol. Biol. , vol.353 , pp. 1093-1105
    • Sun, P.1    Ye, S.2    Ferrandon, S.3    Evans, T.C.4    Xu, M.Q.5    Rao, Z.6


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