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Volumn 135, Issue 2, 2004, Pages 185-191

Interaction of the Escherichia coli Lipoprotein NlpI with Periplasmic Prc (Tsp) Protease

Author keywords

Lipoprotein; NlpI; Peptidoglycan; Prc; Spr

Indexed keywords

LIPOPROTEIN; PROTEINASE;

EID: 1842785354     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvh022     Document Type: Article
Times cited : (25)

References (26)
  • 1
    • 0025832094 scopus 로고
    • Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3
    • Hara, H., Yamamoto, Y., Higashitani, A., Suzuki, H., and Nishimura, Y. (1991) Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3. J. Bacteriol. 173, 4799-4813
    • (1991) J. Bacteriol. , vol.173 , pp. 4799-4813
    • Hara, H.1    Yamamoto, Y.2    Higashitani, A.3    Suzuki, H.4    Nishimura, Y.5
  • 2
    • 0024450646 scopus 로고
    • Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli
    • Hara, H., Nishimura, Y., Kato, J., Suzuki, H., Nagasawa, H., Suzuki, A., and Hirota, Y. (1989) Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli. J. Bacteriol. 171, 5882-5889
    • (1989) J. Bacteriol. , vol.171 , pp. 5882-5889
    • Hara, H.1    Nishimura, Y.2    Kato, J.3    Suzuki, H.4    Nagasawa, H.5    Suzuki, A.6    Hirota, Y.7
  • 3
    • 0024439293 scopus 로고
    • Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli
    • Nagasawa, H., Sakagami, Y., Suzuki, A., Suzuki, H., Hara, H., and Hirota, Y. (1989) Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J. Bacteriol. 171, 5890-5893
    • (1989) J. Bacteriol. , vol.171 , pp. 5890-5893
    • Nagasawa, H.1    Sakagami, Y.2    Suzuki, A.3    Suzuki, H.4    Hara, H.5    Hirota, Y.6
  • 4
    • 0023701409 scopus 로고
    • Lipid modification of Escherichia coli penicillin-binding protein 3
    • Hayashi, S., Hara, H., Suzuki, H., and Hirota, Y. (1988) Lipid modification of Escherichia coli penicillin-binding protein 3. J. Bacteriol. 170, 5392-5395
    • (1988) J. Bacteriol. , vol.170 , pp. 5392-5395
    • Hayashi, S.1    Hara, H.2    Suzuki, H.3    Hirota, Y.4
  • 5
    • 0019206171 scopus 로고
    • On the process of cellular division in Escherichia coli: Isolation and characterization of penicillin-binding proteins 1a, 1b, and 3
    • Tamura, T., Suzuki, H., Nishimura, Y., Mizoguchi, J., and Hirota, Y. (1980) On the process of cellular division in Escherichia coli: Isolation and characterization of penicillin-binding proteins 1a, 1b, and 3. Proc. Natl Acad. Sci. USA 77, 4499-4503
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 4499-4503
    • Tamura, T.1    Suzuki, H.2    Nishimura, Y.3    Mizoguchi, J.4    Hirota, Y.5
  • 6
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K.C., Waller, P.R.H., and Sauer, R.T. (1996) Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271, 990-993
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 7
    • 0029776767 scopus 로고    scopus 로고
    • Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an spr mutation of Escherichia coli
    • Hara, H., Abe, N., Nakakouji, M., Nishimura, Y., and Horiuchi, K. (1996) Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an spr mutation of Escherichia coli. Microb. Drug Resist. 2, 63-72
    • (1996) Microb. Drug Resist. , vol.2 , pp. 63-72
    • Hara, H.1    Abe, N.2    Nakakouji, M.3    Nishimura, Y.4    Horiuchi, K.5
  • 9
    • 0000587078 scopus 로고    scopus 로고
    • (Neidhardt, F.C., Curtiss, R. III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. Umbarger, H.E., eds.) 2nd ed., ASM Press, Washington, DC
    • Wu, H.C. (1996) Biosynthesis of lipoproteins in Neidhardt Escherichia coli and Salmonella: Cellular and Molecular Biology (Neidhardt, F.C., Curtiss, R. III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M. Umbarger, H.E., eds.) 2nd ed., pp. 1005-1014, ASM Press, Washington, DC
    • (1996) Biosynthesis of Lipoproteins in Neidhardt Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1005-1014
    • Wu, H.C.1
  • 10
    • 0027991987 scopus 로고
    • Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase
    • Romeis, T. and Höltje, J.V. (1994) Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase. Eur. J. Biochem. 224, 597-604
    • (1994) Eur. J. Biochem. , vol.224 , pp. 597-604
    • Romeis, T.1    Höltje, J.V.2
  • 11
    • 0026569755 scopus 로고
    • Purification and partial characterization of the γ -D-glutamyl-L-di-amino acid endopeptidase II from Bacillus sphaericus
    • Bourgogne, T., Vacheron, M.J., Guinand, M., and Michel, G. (1992) Purification and partial characterization of the γ-D-glutamyl-L-di-amino acid endopeptidase II from Bacillus sphaericus. Int. J. Biochem. 24, 471-476
    • (1992) Int. J. Biochem. , vol.24 , pp. 471-476
    • Bourgogne, T.1    Vacheron, M.J.2    Guinand, M.3    Michel, G.4
  • 12
    • 0026823415 scopus 로고
    • Cloning and nucleotide sequence of the gene encoding the γ-D-glutamyl-L-diamino acid endopeptidase II of Bacillus sphaericus
    • Hourdou, M.L., Duez, C., Joris, B., Vacheron, M.J., Guinand, M., Michel, G., and Ghuysen, J.M. (1992) Cloning and nucleotide sequence of the gene encoding the γ-D-glutamyl-L-diamino acid endopeptidase II of Bacillus sphaericus. FEMS Microbiol. Lett. 91, 165-170
    • (1992) FEMS Microbiol. Lett. , vol.91 , pp. 165-170
    • Hourdou, M.L.1    Duez, C.2    Joris, B.3    Vacheron, M.J.4    Guinand, M.5    Michel, G.6    Ghuysen, J.M.7
  • 13
    • 0032808952 scopus 로고    scopus 로고
    • Identification and characterization of a new lipoprotein, NlpI, in Escherichia coli K-12
    • Ohara, M., Wu, H.C., Sankaran, K., and Rick, P.D. (1999) Identification and characterization of a new lipoprotein, NlpI, in Escherichia coli K-12. J. Bacteriol. 181, 4318-4325
    • (1999) J. Bacteriol. , vol.181 , pp. 4318-4325
    • Ohara, M.1    Wu, H.C.2    Sankaran, K.3    Rick, P.D.4
  • 14
    • 0031924072 scopus 로고    scopus 로고
    • Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli
    • Murphy, K.C. (1998) Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli. J. Bacteriol. 180, 2063-2071
    • (1998) J. Bacteriol. , vol.180 , pp. 2063-2071
    • Murphy, K.C.1
  • 15
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., Ochs, B., and Abel, K.J. (1988) Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69, 301-315
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 16
    • 0025088052 scopus 로고
    • Low copy number plasmids for regulated low-level expression of cloned genes in Eschirichia coli with blue/white insert screening capability
    • Lerner, C.G. and Inouye, M. (1990) Low copy number plasmids for regulated low-level expression of cloned genes in Eschirichia coli with blue/white insert screening capability. Nucleic Acids Res. 18, 4631
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4631
    • Lerner, C.G.1    Inouye, M.2
  • 17
    • 0028828710 scopus 로고
    • New plasmids carrying antibiotic-resistance cassettes
    • Reece, K.S. and Phillips, G.J. (1995) New plasmids carrying antibiotic-resistance cassettes. Gene 165, 141-142
    • (1995) Gene , vol.165 , pp. 141-142
    • Reece, K.S.1    Phillips, G.J.2
  • 18
    • 0002802808 scopus 로고
    • Mutants of Escherichia coli requiring methionine or vitamin B12
    • Davis, B.D. and Mingioli, E.S. (1950) Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bacteriol. 60, 17-28
    • (1950) J. Bacteriol. , vol.60 , pp. 17-28
    • Davis, B.D.1    Mingioli, E.S.2
  • 19
    • 0028004414 scopus 로고
    • Intrinsic and extrinsic approaches for detecting genes in a bacterial genome
    • Borodovsky, M., Rudd, K.E., and Koonin, E.V. (1994) Intrinsic and extrinsic approaches for detecting genes in a bacterial genome. Nucleic Acids Res. 22, 4756-4767
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4756-4767
    • Borodovsky, M.1    Rudd, K.E.2    Koonin, E.V.3
  • 20
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das, A.K., Cohen, P.T.W., and Barford, D. (1998) The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17, 1192-1199
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.T.W.2    Barford, D.3
  • 21
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: To TPR or not to TPR?
    • Lamb, J.R., Tugendreich, S., and Hieter, P. (1995) Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends Biochem. Sci. 20, 257-259
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 22
    • 0034473417 scopus 로고    scopus 로고
    • Interaction of the nucleoid-associated proteins Hha and H-NS to modulate expression of the hemolysin operon in Escherichia coli
    • Juàrez, A., Nieto, J.M., Prenafeta, A., Miquelay, E., Balsalobre, C., Carrascal, M., and Madrid, C. (2000) Interaction of the nucleoid-associated proteins Hha and H-NS to modulate expression of the hemolysin operon in Escherichia coli. Adv. Exp. Med. Biol. 485, 127-131
    • (2000) Adv. Exp. Med. Biol. , vol.485 , pp. 127-131
    • Juàrez, A.1    Nieto, J.M.2    Prenafeta, A.3    Miquelay, E.4    Balsalobre, C.5    Carrascal, M.6    Madrid, C.7
  • 23
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993) Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 24
    • 0036315595 scopus 로고    scopus 로고
    • Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants
    • Kitagawa, M., Miyakawa, M., Matsumura, Y., and Tsuchido, T. (2002) Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants. Eur. J. Biochem. 269, 2907-2917
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2907-2917
    • Kitagawa, M.1    Miyakawa, M.2    Matsumura, Y.3    Tsuchido, T.4
  • 25
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • Anantharaman, V. and Aravind, L. (2003) Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol. 4, R11
    • (2003) Genome Biol. , vol.4
    • Anantharaman, V.1    Aravind, L.2


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