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Volumn 13, Issue 3, 2004, Pages 443-449

Bivalent Tethering of SspB to ClpXP Is Required for Efficient Substrate Delivery: A Protein-Design Study

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATASE; ATP DEPENDENT ENDOPROTEASE TI; ATP-DEPENDENT ENDOPROTEASE TI; BACTERIAL PROTEIN; CARRIER PROTEIN; DIMER; ENDOPEPTIDASE CLP; ENDOPEPTIDASE CLPX; ENZYME CLPXP; ESCHERICHIA COLI PROTEIN; PEPTIDE FRAGMENT; PROTEIN SSPB; PROTEIN SUBUNIT; SERINE PROTEINASE; SSPB SPECIFICITY FACTOR, E COLI; SSPB SPECIFICITY FACTOR, HEMOPHILUS INFLUENZAE; UNCLASSIFIED DRUG;

EID: 1242271992     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00027-9     Document Type: Article
Times cited : (54)

References (20)
  • 2
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat B.I., Mayo S.L. De novo protein design. fully automated sequence selection Science. 278:1997;82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 3
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • Desmet J., Maeyer M.D., Hazes B., Lasters I. The dead-end elimination theorem and its use in protein side-chain positioning. Nature. 356:1992;539-542.
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    Maeyer, M.D.2    Hazes, B.3    Lasters, I.4
  • 4
    • 1242322964 scopus 로고    scopus 로고
    • Solution structure of the dimeric zinc binding domain of the chaperone ClpX
    • Donaldson L.W., Wojtyra U., Houry W.A. Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J. Biol. Chem. 278:2003;48991-48996.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48991-48996
    • Donaldson, L.W.1    Wojtyra, U.2    Houry, W.A.3
  • 5
    • 0141957392 scopus 로고    scopus 로고
    • Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX
    • Dougan D.A., Weber-Ban E., Bukau B. Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Mol. Cell. 12:2003;373-380.
    • (2003) Mol. Cell , vol.12 , pp. 373-380
    • Dougan, D.A.1    Weber-Ban, E.2    Bukau, B.3
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • Havranek J.J., Harbury P.B. Automated design of specificity in molecular recognition. Nat. Struct. Biol. 10:2003;45-52.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 10
    • 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., 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.2    Sauer, R.T.3
  • 11
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko I., Seidel M., Sauer R.T., Baker T.A. A specificity-enhancing factor for the ClpXP degradation machine. Science. 289:2000;2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 12
    • 0141992126 scopus 로고    scopus 로고
    • Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag
    • Levchenko I., Grant R.A., Wah D.A., Sauer R.T., Baker T.A. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Mol. Cell. 12:2003;365-372.
    • (2003) Mol. Cell , vol.12 , pp. 365-372
    • Levchenko, I.1    Grant, R.A.2    Wah, D.A.3    Sauer, R.T.4    Baker, T.A.5
  • 13
    • 0345687188 scopus 로고    scopus 로고
    • Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate-processing by the ClpXP protease
    • Neher S.B., Sauer R.T., Baker T.A. Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate-processing by the ClpXP protease. Proc. Natl. Acad. Sci. USA. 100:2003;13219-13224.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13219-13224
    • Neher, S.B.1    Sauer, R.T.2    Baker, T.A.3
  • 14
    • 0001114311 scopus 로고    scopus 로고
    • Conformational splitting: A more powerful criterion for dead-end elimination
    • Pierce N.A., Spriet J.A., Desmet J., Mayo S.L. Conformational splitting. a more powerful criterion for dead-end elimination J. Comput. Chem. 21:2000;999-1009.
    • (2000) J. Comput. Chem. , vol.21 , pp. 999-1009
    • Pierce, N.A.1    Spriet, J.A.2    Desmet, J.3    Mayo, S.L.4
  • 15
    • 0033900165 scopus 로고    scopus 로고
    • Computational design of an integrin I domain stabilized in the open high affinity conformation
    • Shimaoka M., Shifman J.M., Jing H., Takagi J., Mayo S.L., Springer T.A. Computational design of an integrin I domain stabilized in the open high affinity conformation. Nat. Struct. Biol. 7:2000;614-616.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 614-616
    • Shimaoka, M.1    Shifman, J.M.2    Jing, H.3    Takagi, J.4    Mayo, S.L.5    Springer, T.A.6
  • 16
    • 0043128700 scopus 로고    scopus 로고
    • Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine
    • Song H.K., Eck M.J. Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine. Mol. Cell. 12:2003;75-86.
    • (2003) Mol. Cell , vol.12 , pp. 75-86
    • Song, H.K.1    Eck, M.J.2
  • 17
    • 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
  • 18
    • 0141888401 scopus 로고    scopus 로고
    • Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease
    • Wah D.A., Levchenko I., Rieckhof G.E., Bolon D.N., Baker T.A., Sauer R.T. Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell. 12:2003;355-363.
    • (2003) Mol. Cell , vol.12 , pp. 355-363
    • Wah, D.A.1    Levchenko, I.2    Rieckhof, G.E.3    Bolon, D.N.4    Baker, T.A.5    Sauer, R.T.6
  • 19
    • 1242289869 scopus 로고    scopus 로고
    • The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function
    • Wojtyra U.A., Thibault G., Tuite A., Houry W.A. The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function. J. Biol. Chem. 278:2003;48981-48990.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48981-48990
    • Wojtyra, U.A.1    Thibault, G.2    Tuite, A.3    Houry, W.A.4
  • 20
    • 0031884182 scopus 로고    scopus 로고
    • Regulation of proteolysis of the stationary-phase sigma factor RpoS
    • Zhou Y., Gottesman S. Regulation of proteolysis of the stationary-phase sigma factor RpoS. J. Bacteriol. 180:1998;1154-1158.
    • (1998) J. Bacteriol. , vol.180 , pp. 1154-1158
    • Zhou, Y.1    Gottesman, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.