메뉴 건너뛰기




Volumn 288, Issue 19, 2013, Pages 13243-13257

Slippery substrates impair function of a bacterial protease ATPase by unbalancing translocation versus exit

Author keywords

[No Author keywords available]

Indexed keywords

VIRUSES;

EID: 84877693301     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.452524     Document Type: Article
Times cited : (22)

References (44)
  • 1
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin. Proteases in the machine age
    • Pickart, C. M., and Cohen, R. E. (2004) Proteasomes and their kin. Proteases in the machine age. Nat. Rev. 5, 177-187
    • (2004) Nat. Rev , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 2
    • 84861553163 scopus 로고    scopus 로고
    • Functional asymmetries of proteasome translocase pore
    • Erales, J., Hoyt, M. A., Troll, F., and Coffino, P. (2012) Functional asymmetries of proteasome translocase pore. J. Biol. Chem. 287, 18535-18543
    • (2012) J. Biol. Chem , vol.287 , pp. 18535-18543
    • Erales, J.1    Hoyt, M.A.2    Troll, F.3    Coffino, P.4
  • 3
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch, J., Fenton, W. A., Furtak, K. J., Farr, G. W., and Horwich, A. L. (2005) Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 4
    • 55549088522 scopus 로고    scopus 로고
    • + ClpX machine grip substrates to drive translocation and unfolding
    • + ClpX machine grip substrates to drive translocation and unfolding. Nat. Struct. Mol. Biol. 15, 1147-1151
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 1147-1151
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 5
    • 79953888421 scopus 로고    scopus 로고
    • Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine
    • Aubin-Tam, M.-E., Olivares, A. O., Sauer, R. T., Baker, T. A., and Lang, M. J. (2011) Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Cell 145, 257-267
    • (2011) Cell , vol.145 , pp. 257-267
    • Aubin-Tam, M.-E.1    Olivares, A.O.2    Sauer, R.T.3    Baker, T.A.4    Lang, M.J.5
  • 8
    • 79955947361 scopus 로고    scopus 로고
    • Dependence of proteasome processing rate on substrate unfolding
    • Henderson, A., Erales, J., Hoyt, M. A., and Coffino, P. (2011) Dependence of proteasome processing rate on substrate unfolding. J. Biol. Chem. 286, 17495-17502
    • (2011) J. Biol. Chem , vol.286 , pp. 17495-17502
    • Henderson, A.1    Erales, J.2    Hoyt, M.A.3    Coffino, P.4
  • 10
    • 13444306170 scopus 로고    scopus 로고
    • Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing
    • Kenniston, J. A., Baker, T. A., and Sauer, R. T. (2005) Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing. Proc. Natl. Acad. Sci. U.S.A. 102, 1390-1395
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 1390-1395
    • Kenniston, J.A.1    Baker, T.A.2    Sauer, R.T.3
  • 11
    • 33846216003 scopus 로고    scopus 로고
    • Proteasome substrate degradation requires association plus extended peptide
    • Takeuchi, J., Chen, H., and Coffino, P. (2007) Proteasome substrate degradation requires association plus extended peptide. EMBO J. 26, 123-131
    • (2007) EMBO J , vol.26 , pp. 123-131
    • Takeuchi, J.1    Chen, H.2    Coffino, P.3
  • 12
    • 0026066613 scopus 로고
    • Generation of p50 subunit of NF-κB by processing of p105 through an ATP-dependent pathway
    • Fan, C. M., and Maniatis, T. (1991) Generation of p50 subunit of NF-κB by processing of p105 through an ATP-dependent pathway. Nature 354, 395-398
    • (1991) Nature , vol.354 , pp. 395-398
    • Fan, C.M.1    Maniatis, T.2
  • 13
    • 1542305655 scopus 로고    scopus 로고
    • Repeat sequence of Epstein-Barr virusencoded nuclear antigen 1 protein interrupts proteasome substrate processing
    • Zhang, M., and Coffino, P. (2004) Repeat sequence of Epstein-Barr virusencoded nuclear antigen 1 protein interrupts proteasome substrate processing. J. Biol. Chem. 279, 8635-8641
    • (2004) J. Biol. Chem , vol.279 , pp. 8635-8641
    • Zhang, M.1    Coffino, P.2
  • 14
    • 2442645033 scopus 로고    scopus 로고
    • Proteasomes begin ornithine decarboxylase digestion at the C terminus
    • Zhang, M., MacDonald, A. I., Hoyt, M. A., and Coffino, P. (2004) Proteasomes begin ornithine decarboxylase digestion at the C terminus. J. Biol. Chem. 279, 20959-20965
    • (2004) J. Biol. Chem , vol.279 , pp. 20959-20965
    • Zhang, M.1    MacDonald, A.I.2    Hoyt, M.A.3    Coffino, P.4
  • 15
    • 33646152750 scopus 로고    scopus 로고
    • Glycine-alanine repeats impair proper substrate unfolding by the proteasome
    • Hoyt, M. A., Zich, J., Takeuchi, J., Zhang, M., Govaerts, C., and Coffino, P. (2006) Glycine-alanine repeats impair proper substrate unfolding by the proteasome. EMBO J. 25, 1720-1729
    • (2006) EMBO J , vol.25 , pp. 1720-1729
    • Hoyt, M.A.1    Zich, J.2    Takeuchi, J.3    Zhang, M.4    Govaerts, C.5    Coffino, P.6
  • 16
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasomemediated degradation
    • Prakash, S., Tian, L., Ratliff, K. S., Lehotzky, R. E., and Matouschek, A. (2004) An unstructured initiation site is required for efficient proteasomemediated degradation. Nat. Struct. Mol. Biol. 11, 830-837
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 18
    • 27144474906 scopus 로고    scopus 로고
    • + motors reveal operating principles for ATP-fuelled machines
    • + motors reveal operating principles for ATP-fuelled machines. Nature 437, 1115-1120
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 19
    • 0031961776 scopus 로고    scopus 로고
    • Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition
    • Jones, J. M., Welty, D. J., and Nakai, H. (1998) Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition. J. Biol. Chem. 273, 459-465
    • (1998) J. Biol. Chem , vol.273 , pp. 459-465
    • Jones, J.M.1    Welty, D.J.2    Nakai, H.3
  • 22
    • 65249086717 scopus 로고    scopus 로고
    • Site-specific protein labeling via sortase-mediated transpeptidation
    • Chapter 15, Unit 15.13
    • Popp, M. W., Antos, J. M., and Ploegh, H. L. (2009) Site-specific protein labeling via sortase-mediated transpeptidation. Curr. Protoc. Protein Sci., Chapter 15, Unit 15.13
    • (2009) Curr. Protoc. Protein Sci
    • Popp, M.W.1    Antos, J.M.2    Ploegh, H.L.3
  • 24
    • 0037143697 scopus 로고    scopus 로고
    • ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence
    • Hoskins, J. R., Yanagihara, K., Mizuuchi, K., and Wickner, S. (2002) ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence. Proc. Natl. Acad. Sci. U.S.A. 99, 11037-11042
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11037-11042
    • Hoskins, J.R.1    Yanagihara, K.2    Mizuuchi, K.3    Wickner, S.4
  • 25
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., Roche, E., Zhou, Y., and Sauer, R. T. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12, 1338-1347
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 26
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers, M., and Schatz, G. (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322, 228-232
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 27
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band. Extensible components of muscle elasticity
    • Improta, S., Politou, A. S., and Pastore, A. (1996) Immunoglobulin-like modules from titin I-band. Extensible components of muscle elasticity. Structure 4, 323-337
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 28
    • 0042839620 scopus 로고    scopus 로고
    • Titin. Properties and family relationships
    • Tskhovrebova, L., and Trinick, J. (2003) Titin. Properties and family relationships. Nat. Rev. 4, 679-689
    • (2003) Nat. Rev , vol.4 , pp. 679-689
    • Tskhovrebova, L.1    Trinick, J.2
  • 30
    • 0028907913 scopus 로고
    • The role of repetitive DNA sequences in the size variation of Epstein-Barr virus (EBV) nuclear antigens and the identification of different EBV isolates using RFLP and PCR analysis
    • Falk, K., Gratama, J. W., Rowe, M., Zou, J. Z., Khanim, F., Young, L. S., Oosterveer, M. A., and Ernberg, I. (1995) The role of repetitive DNA sequences in the size variation of Epstein-Barr virus (EBV) nuclear antigens and the identification of different EBV isolates using RFLP and PCR analysis. J. Gen. Virol. 76, 779-790
    • (1995) J. Gen. Virol , vol.76 , pp. 779-790
    • Falk, K.1    Gratama, J.W.2    Rowe, M.3    Zou, J.Z.4    Khanim, F.5    Young, L.S.6    Oosterveer, M.A.7    Ernberg, I.8
  • 31
    • 0031904016 scopus 로고    scopus 로고
    • A minimal glycine-alanine repeat prevents the interaction of ubiquitinated i κb α with the proteasome. A new mechanism for selective inhibition of proteolysis
    • Sharipo, A., Imreh, M., Leonchiks, A., Imreh, S., and Masucci, M. G. (1998) A minimal glycine-alanine repeat prevents the interaction of ubiquitinated I κB α with the proteasome. A new mechanism for selective inhibition of proteolysis. Nat. Med. 4, 939-944
    • (1998) Nat. Med , vol.4 , pp. 939-944
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Imreh, S.4    Masucci, M.G.5
  • 33
    • 0033539690 scopus 로고    scopus 로고
    • ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease
    • Singh, S. K., Guo, F., and Maurizi, M. R. (1999) ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease. Biochemistry 38, 14906-14915
    • (1999) Biochemistry , vol.38 , pp. 14906-14915
    • Singh, S.K.1    Guo, F.2    Maurizi, M.R.3
  • 34
    • 0034103269 scopus 로고    scopus 로고
    • EBNA-1. A protein pivotal to latent infection by Epstein-Barr virus
    • Leight, E. R., and Sugden, B. (2000) EBNA-1. A protein pivotal to latent infection by Epstein-Barr virus. Rev. Med. Virol. 10, 83-100
    • (2000) Rev. Med. Virol , vol.10 , pp. 83-100
    • Leight, E.R.1    Sugden, B.2
  • 35
    • 0041971307 scopus 로고    scopus 로고
    • Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1
    • Yin, Y., Manoury, B., and Fåhraeus, R. (2003) Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1. Science 301, 1371-1374
    • (2003) Science , vol.301 , pp. 1371-1374
    • Yin, Y.1    Manoury, B.2    Fåhraeus, R.3
  • 36
    • 0035875767 scopus 로고    scopus 로고
    • Cis-Inhibition of proteasomal degradation by viral repeats. Impact of length and amino acid composition
    • Sharipo, A., Imreh, M., Leonchiks, A., Brändén, C., and Masucci, M. G. (2001) cis-Inhibition of proteasomal degradation by viral repeats. Impact of length and amino acid composition. FEBS Lett. 499, 137-142
    • (2001) FEBS Lett , vol.499 , pp. 137-142
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Brändén, C.4    Masucci, M.G.5
  • 37
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
    • Kloetzel, P. M., and Ossendorp, F. (2004) Proteasome and peptidase function in MHC-class-I-mediated antigen presentation. Curr. Opin. Immunol. 16, 76-81
    • (2004) Curr. Opin. Immunol , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 38
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 40
    • 28544434064 scopus 로고    scopus 로고
    • A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB
    • Tian, L., Holmgren, R. A., and Matouschek, A. (2005) A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB. Nat. Struct. Mol. Biol. 12, 1045-1053
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1045-1053
    • Tian, L.1    Holmgren, R.A.2    Matouschek, A.3
  • 42
    • 0026669807 scopus 로고
    • Prediction of the activity and stability effects of site-directed mutagenesis on a protein core
    • van Gunsteren, W. F., and Mark, A. E. (1992) Prediction of the activity and stability effects of site-directed mutagenesis on a protein core. J. Mol. Biol. 227, 389-395
    • (1992) J. Mol. Biol , vol.227 , pp. 389-395
    • Van Gunsteren, W.F.1    Mark, A.E.2
  • 43
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 44
    • 0014349825 scopus 로고
    • The characterization of amino acid sequences in proteins by statistical methods
    • Zimmerman, J. M., Eliezer, N., and Simha, R. (1968) The characterization of amino acid sequences in proteins by statistical methods. J. Theor. Biol. 21, 170-201
    • (1968) J. Theor. Biol , vol.21 , pp. 170-201
    • Zimmerman, J.M.1    Eliezer, N.2    Simha, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.