메뉴 건너뛰기




Volumn 114, Issue 4, 2003, Pages 511-520

Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTEINASE;

EID: 0042329502     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00612-3     Document Type: Article
Times cited : (246)

References (36)
  • 1
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y., Sosnick T.R., Mayne L., Englander S.W. Protein folding intermediates. native-state hydrogen exchange Science. 269:1995;192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 2
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • Benaroudj N., Zwickl P., Seemuller E., Baumeister W., Goldberg A.L. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell. 11:2003;69-78.
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemuller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 3
    • 0035875890 scopus 로고    scopus 로고
    • Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
    • a
    • Burton R.E., Siddiqui S.M., Kim Y.I., Baker T.A., Sauer R.T. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J. 20:2001;3092-3100. a.
    • (2001) EMBO J. , vol.20 , pp. 3092-3100
    • Burton, R.E.1    Siddiqui, S.M.2    Kim, Y.I.3    Baker, T.A.4    Sauer, R.T.5
  • 4
    • 0034840284 scopus 로고    scopus 로고
    • ClpX-mediated remodeling of mu transposasomes: Selective unfolding of subunits destabilizes the entire complex
    • b
    • Burton B.M., Williams T.L., Baker T.A. ClpX-mediated remodeling of mu transposasomes. selective unfolding of subunits destabilizes the entire complex Mol. Cell. 8:2001;449-454. b.
    • (2001) Mol. Cell , vol.8 , pp. 449-454
    • Burton, B.M.1    Williams, T.L.2    Baker, T.A.3
  • 5
    • 0037407940 scopus 로고    scopus 로고
    • Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing
    • Burton R.E., Baker T.A., Sauer R.T. Energy-dependent degradation. linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing Protein Sci. 12:2003;893-902.
    • (2003) Protein Sci. , vol.12 , pp. 893-902
    • Burton, R.E.1    Baker, T.A.2    Sauer, R.T.3
  • 8
    • 0029746061 scopus 로고    scopus 로고
    • Detection of partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain A.K., Handel T.M., Marqusee S. Detection of partially folded molecules in equilibrium with the native conformation of RNaseH. Nat. Struct. Biol. 3:1996;782-787.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 9
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn J.M., Neher S.B., Kim Y.I., Sauer R.T., Baker T.A. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell. 11:2003;671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 10
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • Fowler S.B., Clarke J. Mapping the folding pathway of an immunoglobulin domain. structural detail from phi value analysis and movement of the transition state Structure. 9:2001;355-366.
    • (2001) Structure , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 11
    • 0036389817 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics, NMR and protein engineering
    • Fowler S.B., Best R.B., Toca Herrera J.L., Rutherford T.J., Steward A., Paci E., Karplus M., Clarke J. Mechanical unfolding of a titin Ig domain. structure of unfolding intermediate revealed by combining AFM, molecular dynamics, NMR and protein engineering J. Mol. Biol. 322:2002;841-849.
    • (2002) J. Mol. Biol. , vol.322 , pp. 841-849
    • Fowler, S.B.1    Best, R.B.2    Toca Herrera, J.L.3    Rutherford, T.J.4    Steward, A.5    Paci, E.6    Karplus, M.7    Clarke, J.8
  • 13
    • 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., Sauer R.T. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1998;1338-1347.
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 14
    • 0344211512 scopus 로고    scopus 로고
    • Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH
    • Herman C., Prakash S., Lu C.Z., Matouschek A., Gross C.A. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Mol. Cell. 11:2003;659-669.
    • (2003) Mol. Cell , vol.11 , pp. 659-669
    • Herman, C.1    Prakash, S.2    Lu, C.Z.3    Matouschek, A.4    Gross, C.A.5
  • 15
    • 0033598719 scopus 로고    scopus 로고
    • Structural distribution of stability in a thermophilic enzyme
    • Hollien J., Marqusee S. Structural distribution of stability in a thermophilic enzyme. Proc. Natl. Acad. Sci. USA. 96:1999;13674-13678.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13674-13678
    • Hollien, J.1    Marqusee, S.2
  • 16
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta S., Politou A.S., Pastore A. Immunoglobulin-like modules from titin I-band. extensible components of muscle elasticity Structure. 4:1996;323-337.
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 17
    • 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., Sauer R.T. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science. 271:1996;990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 18
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim Y.I., Burton R.E., Burton B.M., Sauer R.T., Baker T.A. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell. 5:2000;639-648.
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 19
    • 0034194179 scopus 로고    scopus 로고
    • AAA proteases: Cellular machines for degrading membrane proteins
    • Langer T. AAA proteases. cellular machines for degrading membrane proteins Trends Biochem. Sci. 25:2000;247-251.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 247-251
    • Langer, T.1
  • 20
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee C., Schwartz M.P., Prakash S., Iwakura M., Matouschek A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell. 7:2001;627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 22
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Liu H., Isralewitz B., Krammer A., Vogel V., Schulten K. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75:1998;662-671.
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Liu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 25
    • 0037308999 scopus 로고    scopus 로고
    • Protein unfolding - an important process in vivo?
    • Matouschek A. Protein unfolding - an important process in vivo? Curr. Opin. Struct. Biol. 13:2003;98-109.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 98-109
    • Matouschek, A.1
  • 26
    • 0032969563 scopus 로고    scopus 로고
    • Aaa+: A class of chaperone-like atpases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. Aaa+. a class of chaperone-like atpases associated with the assembly, operation, and disassembly of protein complexes Genome Res. 9:1999;27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 27
    • 0023809599 scopus 로고
    • +-ATPase activity
    • +-ATPase activity. Methods Enzymol. 156:1988;116-119.
    • (1988) Methods Enzymol. , vol.156 , pp. 116-119
    • Norby, J.G.1
  • 28
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T., Wilkinson A.J. AAA+ superfamily ATPases. common structure-diverse function Genes Cells. 6:2001;575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 29
    • 0037119954 scopus 로고    scopus 로고
    • Alternating translocation of protein substrates from both ends of ClpXP protease
    • Ortega J., Lee H.S., Maurizi M.R., Steven A.C. Alternating translocation of protein substrates from both ends of ClpXP protease. EMBO J. 21:2002;4938-4949.
    • (2002) EMBO J. , vol.21 , pp. 4938-4949
    • Ortega, J.1    Lee, H.S.2    Maurizi, M.R.3    Steven, A.C.4
  • 30
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl-chymotrypsin using different denaturants
    • Santoro M.M., Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 32
    • 0028305742 scopus 로고
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates
    • Thompson M.W., Maurizi M.R. Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. J. Biol. Chem. 269:1994;18201-18208.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18201-18208
    • Thompson, M.W.1    Maurizi, M.R.2
  • 33
    • 0028365133 scopus 로고
    • Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis
    • Thompson M.W., Singh S.K., Maurizi M.R. Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis. J. Biol. Chem. 269:1994;18209-18215.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18209-18215
    • Thompson, M.W.1    Singh, S.K.2    Maurizi, M.R.3
  • 34
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale R.D. AAA proteins. Lords of the ring. J. Cell Biol. 150:2000;13-19.
    • (2000) J. Cell Biol. , vol.150 , pp. 13-19
    • Vale, R.D.1
  • 35
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah D.A., Levchenko I., Baker T.A., Sauer R.T. Characterization of a specificity factor for an AAA+ ATPase. assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer Chem. Biol. 9:2002;1237-1245.
    • (2002) Chem. Biol. , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 36
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang J., Hartling J.A., Flanagan J.M. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell. 91:1997;447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.