메뉴 건너뛰기




Volumn 488, Issue C, 2011, Pages 239-264

Application of the sequential n-step kinetic mechanism to polypeptide translocases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; MOLECULAR MOTOR; POLYPEPTIDE;

EID: 78650955824     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381268-1.00010-0     Document Type: Chapter
Times cited : (11)

References (29)
  • 1
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • J.A. Ali, and T.M. Lohman Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase Science 275 1997 377 380
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 2
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • S.M. Block Bead movement by single kinesin molecules studied with optical tweezers Nature 348 1990 348 352
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1
  • 3
    • 0024413057 scopus 로고
    • ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin
    • E. Eytan ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin Proc. Natl. Acad. Sci. USA 86 1989 7751 7755
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7751-7755
    • Eytan, E.1
  • 4
    • 9244237061 scopus 로고    scopus 로고
    • ATP-dependent translocation of proteins along single-stranded DNA: Models and methods of analysis of pre-steady state kinetics
    • C.J. Fischer, and T.M. Lohman ATP-dependent translocation of proteins along single-stranded DNA: Models and methods of analysis of pre-steady state kinetics J. Mol. Biol. 344 2004 1265 1286
    • (2004) J. Mol. Biol. , vol.344 , pp. 1265-1286
    • Fischer, C.J.1    Lohman, T.M.2
  • 5
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA
    • C.J. Fischer Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA J. Mol. Biol. 344 2004 1287 1309
    • (2004) J. Mol. Biol. , vol.344 , pp. 1287-1309
    • Fischer, C.J.1
  • 6
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • J.R. Glover, and S. Lindquist Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins Cell 94 1998 73 82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 7
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • P. Goloubinoff Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network Proc. Natl. Acad. Sci. USA 96 1999 13732 13737
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1
  • 8
    • 0034255124 scopus 로고    scopus 로고
    • Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
    • J.R. Hoskins Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP Proc. Natl. Acad. Sci. USA 97 2000 8892 8897
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8892-8897
    • Hoskins, J.R.1
  • 9
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • R. Hough Purification of two high molecular weight proteases from rabbit reticulocyte lysate J. Biol. Chem. 262 1987 8303 8313
    • (1987) J. Biol. Chem. , vol.262 , pp. 8303-8313
    • Hough, R.1
  • 10
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • J. Howard Movement of microtubules by single kinesin molecules Nature 342 1989 154 158
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1
  • 11
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • E. Jankowsky The DExH protein NPH-II is a processive and directional motor for unwinding RNA Nature 403 2000 447 451
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1
  • 12
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Y.I. Kim 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
  • 14
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • T.M. Lohman, and K.P. Bjornson Mechanisms of helicase-catalyzed DNA unwinding Annu. Rev. Biochem. 65 1996 169 214
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 15
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • T.M. Lohman Non-hexameric DNA helicases and translocases: Mechanisms and regulation Nat. Rev. Mol. Cell Biol. 9 2008 391 401
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 391-401
    • Lohman, T.M.1
  • 16
    • 0036447339 scopus 로고    scopus 로고
    • DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies
    • A.L. Lucius DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies J. Mol. Biol. 324 2002 409 428
    • (2002) J. Mol. Biol. , vol.324 , pp. 409-428
    • Lucius, A.L.1
  • 17
    • 0141865611 scopus 로고    scopus 로고
    • General methods for analysis of sequential "n-step" kinetic mechanisms: Application to single turnover kinetics of helicase-catalyzed DNA unwinding
    • A.L. Lucius General methods for analysis of sequential "n-step" kinetic mechanisms: Application to single turnover kinetics of helicase-catalyzed DNA unwinding Biophys. J. 85 2003 2224 2239
    • (2003) Biophys. J. , vol.85 , pp. 2224-2239
    • Lucius, A.L.1
  • 18
    • 2542430217 scopus 로고    scopus 로고
    • Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding
    • A.L. Lucius Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding J. Mol. Biol. 339 2004 731 750
    • (2004) J. Mol. Biol. , vol.339 , pp. 731-750
    • Lucius, A.L.1
  • 20
    • 16844376945 scopus 로고    scopus 로고
    • The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer
    • G. Piszczek, J. Rozycki, S.K. Singh, A. Ginsburg, and M.R. Maurizi The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer J. Biol. Chem. 280 2005 12221 12230
    • (2005) J. Biol. Chem. , vol.280 , pp. 12221-12230
    • Piszczek, G.1    Rozycki, J.2    Singh, S.K.3    Ginsburg, A.4    Maurizi, M.R.5
  • 21
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • A.M. Pyle Translocation and unwinding mechanisms of RNA and DNA helicases Annu. Rev. Biophys. 37 2008 317 336
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 22
    • 77953689102 scopus 로고    scopus 로고
    • Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase
    • B. Rajendar, and A.L. Lucius Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase J. Mol. Biol. 399 2010 665 679
    • (2010) J. Mol. Biol. , vol.399 , pp. 665-679
    • Rajendar, B.1    Lucius, A.L.2
  • 23
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 24
    • 0035957317 scopus 로고    scopus 로고
    • ClpA mediates directional translocation of substrate proteins into the ClpP protease
    • B.G. Reid ClpA mediates directional translocation of substrate proteins into the ClpP protease Proc. Natl. Acad. Sci. USA 98 2001 3768 3772
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3768-3772
    • Reid, B.G.1
  • 25
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • K. Svoboda Direct observation of kinesin stepping by optical trapping interferometry Nature 365 1993 721 727
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1
  • 26
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • T.Q. Uyeda Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin J. Mol. Biol. 214 1990 699 710
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.1
  • 28
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • J. Weibezahn Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB Cell 119 2004 653 665
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1
  • 29
    • 54049111011 scopus 로고    scopus 로고
    • Structure of a complex of the ATPase SecA and the protein-translocation channel
    • J. Zimmer Structure of a complex of the ATPase SecA and the protein-translocation channel Nature 455 2008 936 943
    • (2008) Nature , vol.455 , pp. 936-943
    • Zimmer, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.