메뉴 건너뛰기




Volumn 579, Issue 21, 2005, Pages 4707-4712

Importance of a repetitive nine-residue sequence motif for intracellular stability and functional structure of a family I.3 lipase

Author keywords

Roll; Ca 2+ binding; Family I.3 lipase; Mutation; Pseudomonas; Type I secretion system

Indexed keywords

BACTERIAL ENZYME; CALCIUM ION; MUTANT PROTEIN; TRIACYLGLYCEROL LIPASE;

EID: 24044478793     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.07.041     Document Type: Article
Times cited : (27)

References (32)
  • 1
    • 0034704990 scopus 로고    scopus 로고
    • Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp. MIS38
    • K. Amada, M. Haruki, T. Imanaka, M. Morikawa, and S. Kanaya Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp. MIS38 Biochim. Biophys. Acta 1478 2000 201 210
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 201-210
    • Amada, K.1    Haruki, M.2    Imanaka, T.3    Morikawa, M.4    Kanaya, S.5
  • 2
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • J.L. Arpigny, and K.E. Jaeger Bacterial lipolytic enzymes: classification and properties Biochem. J. 343 1999 177 183
    • (1999) Biochem. J. , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 3
    • 0037272519 scopus 로고    scopus 로고
    • Gram-negative bacterial ATP-binding cassette protein exporter family and diverse secretory proteins
    • K. Omori, and A. Idei Gram-negative bacterial ATP-binding cassette protein exporter family and diverse secretory proteins J. Biosci. Bioeng. 95 2003 1 12
    • (2003) J. Biosci. Bioeng. , vol.95 , pp. 1-12
    • Omori, K.1    Idei, A.2
  • 4
    • 0022260426 scopus 로고
    • Nucleotide sequence of an Escherichia coli chromosomal hemolysin
    • T. Felmlee, S. Pellett, and R.A. Welch Nucleotide sequence of an Escherichia coli chromosomal hemolysin J. Bacteriol. 163 1985 94 105
    • (1985) J. Bacteriol. , vol.163 , pp. 94-105
    • Felmlee, T.1    Pellett, S.2    Welch, R.A.3
  • 5
    • 0024370667 scopus 로고
    • Protease secretion by Erwinia chrysanthemi. Proteases B and C are synthesized and secreted as zymogens without a signal peptide
    • P. Delepelaire, and C. Wandersman Protease secretion by Erwinia chrysanthemi. Proteases B and C are synthesized and secreted as zymogens without a signal peptide J. Biol. Chem. 264 1989 9083 9089
    • (1989) J. Biol. Chem. , vol.264 , pp. 9083-9089
    • Delepelaire, P.1    Wandersman, C.2
  • 6
    • 0037342768 scopus 로고    scopus 로고
    • Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
    • N. Aghajari, F. Van Petegem, V. Villeret, J.P. Chessa, C. Gerday, R. Haser, and J. van Beeumen Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases Proteins 50 2003 636 647
    • (2003) Proteins , vol.50 , pp. 636-647
    • Aghajari, N.1    Van Petegem, F.2    Villeret, V.3    Chessa, J.P.4    Gerday, C.5    Haser, R.6    Van Beeumen, J.7
  • 7
    • 0026475721 scopus 로고
    • Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: Relationships to other secretory pathways
    • F. Duong, A. Lazdunski, B. Cami, and M. Murgier Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways Gene 121 1992 47 54
    • (1992) Gene , vol.121 , pp. 47-54
    • Duong, F.1    Lazdunski, A.2    Cami, B.3    Murgier, M.4
  • 8
    • 0029954886 scopus 로고    scopus 로고
    • Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a β-sheet coil motif at 2.0 Å resolution
    • K. Hamada, Y. Hata, Y. Katsuya, H. Hiramatsu, T. Fujiwara, and Y. Katsube Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a β-sheet coil motif at 2.0 Å resolution J. Biochem. 119 1996 844 851
    • (1996) J. Biochem. , vol.119 , pp. 844-851
    • Hamada, K.1    Hata, Y.2    Katsuya, Y.3    Hiramatsu, H.4    Fujiwara, T.5    Katsube, Y.6
  • 9
    • 0028027226 scopus 로고
    • Crystal structure of the 50 kDa metallo protease from Serratia marcescens
    • U. Baumann Crystal structure of the 50 kDa metallo protease from Serratia marcescens J. Mol. Biol. 242 1994 244 251
    • (1994) J. Mol. Biol. , vol.242 , pp. 244-251
    • Baumann, U.1
  • 10
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • U. Baumann, S. Wu, K.M. Flaherty, and D.B. McKay Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif EMBO J. 12 1993 3357 3364
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 11
    • 0029161756 scopus 로고
    • Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding
    • H. Miyatake, Y. Hata, T. Fujii, K. Hamada, K. Morihara, and Y. Katsube Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding J. Biochem. 118 1995 474 479
    • (1995) J. Biochem. , vol.118 , pp. 474-479
    • Miyatake, H.1    Hata, Y.2    Fujii, T.3    Hamada, K.4    Morihara, K.5    Katsube, Y.6
  • 12
    • 0035941112 scopus 로고    scopus 로고
    • Protease C of Erwinia chrysanthemi: The crystal structure and role of amino acids Y228 and E189
    • T. Hege, and U. Baumann Protease C of Erwinia chrysanthemi: the crystal structure and role of amino acids Y228 and E189 J. Mol. Biol. 313 2001 187 193
    • (2001) J. Mol. Biol. , vol.313 , pp. 187-193
    • Hege, T.1    Baumann, U.2
  • 13
    • 0036202210 scopus 로고    scopus 로고
    • Role of repetitive nine-residue sequence motifs in secretion, enzymatic activity, and protein conformation of a family I.3 lipase
    • H.J. Kwon, M. Haruki, M. Morikawa, and S. Kanaya Role of repetitive nine-residue sequence motifs in secretion, enzymatic activity, and protein conformation of a family I.3 lipase J. Biosci. Bioeng. 93 2002 157 164
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 157-164
    • Kwon, H.J.1    Haruki, M.2    Morikawa, M.3    Kanaya, S.4
  • 14
    • 0028292373 scopus 로고
    • A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway
    • J.M. Ghigo, and C. Wandersman A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway J. Biol. Chem. 269 1994 8979 8985
    • (1994) J. Biol. Chem. , vol.269 , pp. 8979-8985
    • Ghigo, J.M.1    Wandersman, C.2
  • 15
    • 0035920232 scopus 로고    scopus 로고
    • Serratia ATP-binding cassette protein exporter, Lip, recognizes a protein region upstream of the C terminus for specific secretion
    • K. Omori, A. Idei, and H. Akatsuka Serratia ATP-binding cassette protein exporter, Lip, recognizes a protein region upstream of the C terminus for specific secretion J. Biol. Chem. 276 2001 27111 27119
    • (2001) J. Biol. Chem. , vol.276 , pp. 27111-27119
    • Omori, K.1    Idei, A.2    Akatsuka, H.3
  • 16
    • 0029815310 scopus 로고    scopus 로고
    • Protein secretion by heterologous bacterial aBC-transporters: The C-terminus secretion signal of the secreted protein confers high recognition specificity
    • F. Duong, A. Lazdunski, and M. Murgier Protein secretion by heterologous bacterial aBC-transporters: the C-terminus secretion signal of the secreted protein confers high recognition specificity Mol. Microbiol. 21 1996 459 470
    • (1996) Mol. Microbiol. , vol.21 , pp. 459-470
    • Duong, F.1    Lazdunski, A.2    Murgier, M.3
  • 17
    • 0026095620 scopus 로고
    • Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or β-galactosidase fused to the Hly C-terminal signal domain
    • B. Kenny, R. Haigh, and I.B. Holland Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or β-galactosidase fused to the Hly C-terminal signal domain Mol. Microbiol. 5 1991 2557 2568
    • (1991) Mol. Microbiol. , vol.5 , pp. 2557-2568
    • Kenny, B.1    Haigh, R.2    Holland, I.B.3
  • 18
    • 0026780472 scopus 로고
    • Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: Involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B
    • S. Letoffe, and C. Wandersman Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B J. Bacteriol. 174 1992 4920 4927
    • (1992) J. Bacteriol. , vol.174 , pp. 4920-4927
    • Letoffe, S.1    Wandersman, C.2
  • 19
    • 0024041944 scopus 로고
    • Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion
    • T. Felmlee, and R.A. Welch Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion Proc. Natl. Acad. Sci. USA 85 1988 5269 5273
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5269-5273
    • Felmlee, T.1    Welch, R.A.2
  • 20
    • 0025184938 scopus 로고
    • Protein secretion in Gram-negative bacteria. the extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin
    • P. Delepelaire, and C. Wandersman Protein secretion in Gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin J. Biol. Chem. 265 1990 17118 17125
    • (1990) J. Biol. Chem. , vol.265 , pp. 17118-17125
    • Delepelaire, P.1    Wandersman, C.2
  • 21
    • 0031780199 scopus 로고    scopus 로고
    • Serratia marcescens S-layer protein is secreted extracellulary via an ATP-binding cassette exporter, the Lip system
    • E. Kawai, H. Akatsuka, A. Idei, T. Shibatani, and K. Omori Serratia marcescens S-layer protein is secreted extracellulary via an ATP-binding cassette exporter, the Lip system Mol. Microbiol. 27 1998 941 952
    • (1998) Mol. Microbiol. , vol.27 , pp. 941-952
    • Kawai, E.1    Akatsuka, H.2    Idei, A.3    Shibatani, T.4    Omori, K.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 84871693371 scopus 로고
    • The spectrophotometric determination of tyrosine and tryptophan in proteins
    • T.W. Goodwin, and R.A. Morton The spectrophotometric determination of tyrosine and tryptophan in proteins Biochem. J. 40 1946 628 632
    • (1946) Biochem. J. , vol.40 , pp. 628-632
    • Goodwin, T.W.1    Morton, R.A.2
  • 24
    • 0032492721 scopus 로고    scopus 로고
    • 2+ bind to the catalytic domain, but not the C2 domain
    • 2+ bind to the catalytic domain, but not the C2 domain Biochemistry 37 1998 5020 5028
    • (1998) Biochemistry , vol.37 , pp. 5020-5028
    • Grobler, J.A.1    Hurley, J.H.2
  • 26
    • 0028819525 scopus 로고
    • The binding of divalent cations to Escherichia coli alpha-haemolysin
    • H. Ostolaza, A. Soloaga, and F.M. Goni The binding of divalent cations to Escherichia coli alpha-haemolysin Eur. J. Biochem. 228 1995 39 44
    • (1995) Eur. J. Biochem. , vol.228 , pp. 39-44
    • Ostolaza, H.1    Soloaga, A.2    Goni, F.M.3
  • 27
    • 0028877021 scopus 로고
    • Interaction of calcium with Bordetella pertussis adenylate cyclase toxin
    • T. Rose, P. Sebo, J. Bellalou, and D. Ladan Interaction of calcium with Bordetella pertussis adenylate cyclase toxin J. Biol. Chem. 270 1995 26370 36376
    • (1995) J. Biol. Chem. , vol.270 , pp. 26370-36376
    • Rose, T.1    Sebo, P.2    Bellalou, J.3    Ladan, D.4
  • 28
    • 0031891157 scopus 로고    scopus 로고
    • Long-range effect of mutation of calcium binding aspartates on the catalytic activity of alkaline protease from Pseudomonas aeruginosa
    • Y. Miyajima, Y. Hata, J. Fukushima, S. Kawamoto, K. Okuda, Y. Shibano, and K. Morihara Long-range effect of mutation of calcium binding aspartates on the catalytic activity of alkaline protease from Pseudomonas aeruginosa J. Biochem. 123 1998 24 27
    • (1998) J. Biochem. , vol.123 , pp. 24-27
    • Miyajima, Y.1    Hata, Y.2    Fukushima, J.3    Kawamoto, S.4    Okuda, K.5    Shibano, Y.6    Morihara, K.7
  • 29
    • 0141865703 scopus 로고    scopus 로고
    • Self-assembly of proteins into designed networks
    • P. Ringler, and G.E. Schulz Self-assembly of proteins into designed networks Science 302 2003 106 107
    • (2003) Science , vol.302 , pp. 106-107
    • Ringler, P.1    Schulz, G.E.2
  • 31
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • V. Koronakis, A. Sharff, E. Koronakis, B. Luisi, and C. Hughes Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export Nature 405 2000 914 919
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 32
    • 0034693168 scopus 로고    scopus 로고
    • Identification of the histidine and aspartic acid residues essential for enzymatic activity of a family I.3 lipase by site-directed mutagenesis
    • H.J. Kwon, K. Amada, M. Haruki, M. Morikawa, and S. Kanaya Identification of the histidine and aspartic acid residues essential for enzymatic activity of a family I.3 lipase by site-directed mutagenesis FEBS Lett. 483 2000 139 142
    • (2000) FEBS Lett. , vol.483 , pp. 139-142
    • Kwon, H.J.1    Amada, K.2    Haruki, M.3    Morikawa, M.4    Kanaya, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.