메뉴 건너뛰기




Volumn 91, Issue 7, 1997, Pages 939-947

PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HYBRID PROTEIN; PROTEINASE;

EID: 0031457264     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80485-7     Document Type: Article
Times cited : (100)

References (47)
  • 1
    • 0027203762 scopus 로고
    • Division of labor among monomers within the Mu transposase tetramer
    • Baker, T.A., Mizuuchi, M., Savilahti, H., and Mizuuchi, K. (1993). Division of labor among monomers within the Mu transposase tetramer. Cell 74, 723-733.
    • (1993) Cell , vol.74 , pp. 723-733
    • Baker, T.A.1    Mizuuchi, M.2    Savilahti, H.3    Mizuuchi, K.4
  • 2
    • 0030925223 scopus 로고    scopus 로고
    • Crystal structure of heat shock locus V (HslV) from Escherichia coli
    • Bochtler, M., Ditzel, L., Groll, M., and Huber, R. (1997). Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proc. Natl. Acad. Sci. USA 94, 6070-6074.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6070-6074
    • Bochtler, M.1    Ditzel, L.2    Groll, M.3    Huber, R.4
  • 4
    • 0016753879 scopus 로고
    • Pulse methods for the simplification of protein NMR spectra
    • Campbell, I.D., Dobson, C.M., Williams, R.J., and Wright, P.E. (1975). Pulse methods for the simplification of protein NMR spectra. FEBS Lett. 57, 96-99
    • (1975) FEBS Lett. , vol.57 , pp. 96-99
    • Campbell, I.D.1    Dobson, C.M.2    Williams, R.J.3    Wright, P.E.4
  • 6
    • 0026492629 scopus 로고
    • The rat brain post-synaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho, K.O., Hunt, C.A., and Kennedy, M.B. (1992). The rat brain post-synaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9, 929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 7
    • 0029400480 scopus 로고
    • NMRPIPE: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A. (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.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 8
    • 0030747761 scopus 로고    scopus 로고
    • Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle
    • Domian, I.J., Quon, K.C., and Shapiro, L. (1997). Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle. Cell 90, 415-424.
    • (1997) Cell , vol.90 , pp. 415-424
    • Domian, I.J.1    Quon, K.C.2    Shapiro, L.3
  • 9
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M., and MacKinnon, R. (1996). Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85, 1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    Mackinnon, R.6
  • 10
    • 0030293766 scopus 로고    scopus 로고
    • Protein-protein interactions: PDZ domain networks
    • Fanning, A.S., and Anderson, J.M. (1996). Protein-protein interactions: PDZ domain networks. Curr. Biol. 6, 1385-1388.
    • (1996) Curr. Biol. , vol.6 , pp. 1385-1388
    • Fanning, A.S.1    Anderson, J.M.2
  • 13
    • 0025952865 scopus 로고
    • Frameshift mutations in the bacteriophage Mu represser gene can confer a trans-dominant virulent phenotype to the phage
    • Geuskens, V., Vogel, J.L., Grimaud, R., Desmet, L., Higgins, N.P., and Toussaint, A. (1991). Frameshift mutations in the bacteriophage Mu represser gene can confer a trans-dominant virulent phenotype to the phage. J. Bacteriol. 773, 6578-6585.
    • (1991) J. Bacteriol. , vol.773 , pp. 6578-6585
    • Geuskens, V.1    Vogel, J.L.2    Grimaud, R.3    Desmet, L.4    Higgins, N.P.5    Toussaint, A.6
  • 14
    • 0027072504 scopus 로고
    • Virulence in bacteriophage Mu: A case of trans-dominant proteolysis by the Escherichia coli Clp serine protease
    • Geuskens, V., Mhammedi-Alaoui, A., Desmet, L., and Toussaint, A. (1992). Virulence in bacteriophage Mu: a case of trans-dominant proteolysis by the Escherichia coli Clp serine protease. EMBO J. 11, 5121-5127.
    • (1992) EMBO J. , vol.11 , pp. 5121-5127
    • Geuskens, V.1    Mhammedi-Alaoui, A.2    Desmet, L.3    Toussaint, A.4
  • 15
    • 0027364289 scopus 로고
    • ClpX, an alternative subunit for ATP-dependent Clp protease of E. Coli
    • Gottesman, S., Clark, W.P., Crecy-Lagard, V., and Maurizi, M.R. (1993). ClpX, an alternative subunit for ATP-dependent Clp protease of E. coli. J. Biol. Chem. 268, 22618-22626.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22618-22626
    • Gottesman, S.1    Clark, W.P.2    Crecy-Lagard, V.3    Maurizi, M.R.4
  • 16
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison, S.C. (1996). Peptide-surface association: the case of PDZ and PTB domains. Cell 86, 341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 18
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of protein 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 protein synthesized from damaged messenger RNA. Science 277, 990-993.
    • (1996) Science , vol.277 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    And Sauer, R.T.3
  • 19
    • 0029126356 scopus 로고
    • Homology in structural organization between E coli ClpAP protease and the eukaryotic 26 S proteasome
    • Kessel, M., Maurizi, M.R., Kim, B., Kocsis, E., Trus, B., Singh, S.K., and Steven, A.C. (1995). Homology in structural organization between E coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250, 587-594.
    • (1995) J. Mol. Biol. , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Kocsis, E.4    Trus, B.5    Singh, S.K.6    Steven, A.C.7
  • 20
    • 0030020897 scopus 로고    scopus 로고
    • ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
    • Kruklitis, R.,Welty, D.J., and Nakai, H. (1996). ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15, 935-944.
    • (1996) EMBO J. , vol.15 , pp. 935-944
    • Kruklitis, R.1    Welty, D.J.2    Nakai, H.3
  • 21
    • 0030048167 scopus 로고    scopus 로고
    • Bacteriophage Mu represser as a target for the E. Coli ATP-dependent Clp protease
    • Laachouch, J.E., Desmet, L., Geuskens, V., Grimaud, R., and Toussaint, A. (1996). Bacteriophage Mu represser as a target for the E. coli ATP-dependent Clp protease. EMBO J. 15, 437-444.
    • (1996) EMBO J. , vol.15 , pp. 437-444
    • Laachouch, J.E.1    Desmet, L.2    Geuskens, V.3    Grimaud, R.4    Toussaint, A.5
  • 22
    • 0028985596 scopus 로고
    • Addiction protein Phd of plasmid prophage P1 is a substrate of ClpXP serine protease of Escherichia coli
    • Lehnherr, H., and Yarmolinsky, M.B. (1995). Addiction protein Phd of plasmid prophage P1 is a substrate of ClpXP serine protease of Escherichia coli. Proc. Natl. Acad. Sci. USA 92, 3274-3277.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3274-3277
    • Lehnherr, H.1    Yarmolinsky, M.B.2
  • 23
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko, I., Luo, L., and Baker, T.A. (1995). Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9, 2399-2408.
    • (1995) Genes Dev. , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 24
    • 0030908043 scopus 로고    scopus 로고
    • ClpX and MuB interact with overlapping regions of Mu transposase: Implications for control of the transposition pathway
    • Levchenko, I., Yamauchi, M., and Baker, T.A. (1997). ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11, 1561-1572.
    • (1997) Genes Dev. , vol.11 , pp. 1561-1572
    • Levchenko, I.1    Yamauchi, M.2    Baker, T.A.3
  • 25
    • 0028359550 scopus 로고
    • A new component of bacteriophage mu replicative transposition machinery: The Escherichia coli ClpX protein
    • Mhammedi-Alaoui, A., Pato, M., Gama, M., and Toussaint, A. (1994). A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein. Mol. Microbiol. 11, 1109-1116.
    • (1994) Mol. Microbiol. , vol.11 , pp. 1109-1116
    • Mhammedi-Alaoui, A.1    Pato, M.2    Gama, M.3    Toussaint, A.4
  • 26
    • 0027482287 scopus 로고
    • P22 arc represser: Enhanced expression of unstable mutants by addition of polar C-terminal sequences
    • Milla, M.E., Brown, B.M., and Sauer, R.T. (1993). P22 Arc represser: enhanced expression of unstable mutants by addition of polar C-terminal sequences. Protein Sci. 2, 2198-2205.
    • (1993) Protein Sci. , vol.2 , pp. 2198-2205
    • Milla, M.E.1    Brown, B.M.2    Sauer, R.T.3
  • 27
    • 0029097732 scopus 로고
    • Disassembly of the bacteriophage Mu transposase for the initiation of Mu DNA replication
    • Nakai, H., and Kruklitis, R. (1995). Disassembly of the bacteriophage Mu transposase for the initiation of Mu DNA replication. J. Biol. Chem. 270, 19591-19598.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19591-19598
    • Nakai, H.1    Kruklitis, R.2
  • 28
    • 0025777272 scopus 로고
    • Hsp 104 is a highly conserved protein with two essential nucleotide-binding sites
    • Parsell, D.A., Sanchez, Y., Stitzel, J.D., and Lindquist, S. (1991). Hsp 104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353, 270-273.
    • (1991) Nature , vol.353 , pp. 270-273
    • Parsell, D.A.1    Sanchez, Y.2    Stitzel, J.D.3    Lindquist, S.4
  • 29
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D.A., Kowal, A.S., Singer, M.A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-477.
    • (1994) Nature , vol.372 , pp. 475-477
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 30
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in bacteria, yeast, and plants
    • Ponting, C.P. (1997). Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci. 6, 464-468.
    • (1997) Protein Sci. , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 31
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rüdiger, S., Buchberger, A., and Bukau, B. (1997). Interaction of Hsp70 chaperones with substrates. Nature Struct. Biol. 4, 342-349.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 342-349
    • Rüdiger, S.1    Buchberger, A.2    Bukau, B.3
  • 32
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras, J., and Heldin, C.H. (1996). PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem. Sci. 21, 455-458.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.H.2
  • 33
  • 35
    • 0029664550 scopus 로고    scopus 로고
    • 2+ channel by INAD in Drosophila photoreceptors
    • 2+ channel by INAD in Drosophila photoreceptors. Neuron 16, 991-998.
    • (1996) Neuron , vol.16 , pp. 991-998
    • Shieh, B.H.1    Zhu, M.Y.2
  • 38
    • 0023663468 scopus 로고
    • Transpososomes: Stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA
    • Surette, M.G., Buch, S.J., and Chaconas, G. (1987). Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA. Cell 49, 253-262.
    • (1987) Cell , vol.49 , pp. 253-262
    • Surette, M.G.1    Buch, S.J.2    Chaconas, G.3
  • 40
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade
    • Tsunoda, S., Sierralta, J., Sun, Y., Bodner, R., Suzuki, E., Becker, A., Socolich, M., and Zuker, C.S. (1997). A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade. Nature 388, 243-249.
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.3    Bodner, R.4    Suzuki, E.5    Becker, A.6    Socolich, M.7    Zuker, C.S.8
  • 41
    • 0028906813 scopus 로고
    • C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10sa RNA decapeptide
    • Tu, G.F., Reid, G.E., Zhang, J.G., Moritz, R.L., and Simpson, R.J. (1995). C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide. J. Biol. Chem. 270, 9322-9326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9322-9326
    • Tu, G.F.1    Reid, G.E.2    Zhang, J.G.3    Moritz, R.L.4    Simpson, R.J.5
  • 42
    • 0029257254 scopus 로고
    • Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation
    • Vogel, J.L., Parsell, D.A., and Lindquist, S. (1995). Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation. Curr. Biol. 5, 306-317.
    • (1995) Curr. Biol. , vol.5 , pp. 306-317
    • Vogel, J.L.1    Parsell, D.A.2    Lindquist, S.3
  • 43
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., Wojtkowiak, D., Marzalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C., and Zylicz, M. (1995). The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14, 1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marzalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 44
    • 0023160123 scopus 로고
    • 1H NMR aromatic spectrum of the operator binding domain of the lambda represser: Resonance assignment with application to structure and dynamics
    • 1H NMR aromatic spectrum of the operator binding domain of the lambda represser: resonance assignment with application to structure and dynamics. Biochemistry 26, 890-897.
    • (1987) Biochemistry , vol.26 , pp. 890-897
    • Weiss, M.A.1    Karplus, M.2    Sauer, R.T.3
  • 45
    • 0031565724 scopus 로고    scopus 로고
    • Communication of ClpXP protease hypersensitivity to bacteriophage Mu represser isoforms
    • Welty, D.J., Jones, J.M., and Nakai, H. (1997). Communication of ClpXP protease hypersensitivity to bacteriophage Mu represser isoforms. J. Mol. Biol. 272, 31-41.
    • (1997) J. Mol. Biol. , vol.272 , pp. 31-41
    • Welty, D.J.1    Jones, J.M.2    Nakai, H.3
  • 47
    • 0027519423 scopus 로고
    • Isolation and characterization of ClpX, anew ATP-dependent specificity component of ClpP protease of E. Coli
    • Wojtkowiak, D., Georgopoulos, C., and Zylicz, M. (1993). Isolation and characterization of ClpX, anew ATP-dependent specificity component of ClpP protease of E. coli. J. Biol. Chem. 268, 22609-22617.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22609-22617
    • Wojtkowiak, D.1    Georgopoulos, C.2    Zylicz, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.