메뉴 건너뛰기




Volumn 109, Issue 50, 2012, Pages 20431-20436

Single-molecule dissection of the high-affinity cohesin-dockerin complex

Author keywords

Molecular recognition; Protein unfolding

Indexed keywords

CALCIUM ION; CELL PROTEIN; COHESIN; DOCKERIN; EDETIC ACID; UNCLASSIFIED DRUG;

EID: 84870914642     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1211929109     Document Type: Article
Times cited : (105)

References (41)
  • 1
    • 77952257725 scopus 로고    scopus 로고
    • Microbial enzyme systems for biomass conversion: Emerging paradigms
    • Himmel ME, et al. (2010) Microbial enzyme systems for biomass conversion: Emerging paradigms. Biofuels 1(2):323-341.
    • (2010) Biofuels , vol.1 , Issue.2 , pp. 323-341
    • Himmel, M.E.1
  • 3
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer EA, Belaich JP, Shoham Y, Lamed R (2004) The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides. Annu Rev Microbiol 58:521- 554.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.P.2    Shoham, Y.3    Lamed, R.4
  • 4
    • 40449093567 scopus 로고    scopus 로고
    • Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: Insight into cellulosome assembly revealed by systematic mutagenesis
    • DOI 10.1042/BJ20071193
    • Karpol A, Barak Y, Lamed R, Shoham Y, Bayer EA (2008) Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: Insight into cellulosome assembly revealed by systematic mutagenesis. Biochem J 410(2):331-338. (Pubitemid 351346191)
    • (2008) Biochemical Journal , vol.410 , Issue.2 , pp. 331-338
    • Karpol, A.1    Barak, Y.2    Lamed, R.3    Shoham, Y.4    Bayer, E.A.5
  • 6
    • 78049440008 scopus 로고    scopus 로고
    • Characterization of a dockerin-based affinity tag: Application for purification of a broad variety of target proteins
    • Demishtein A, Karpol A, Barak Y, Lamed R, Bayer EA (2010) Characterization of a dockerin-based affinity tag: Application for purification of a broad variety of target proteins. J Mol Recognit 23(6):525-535.
    • (2010) J Mol Recognit , vol.23 , Issue.6 , pp. 525-535
    • Demishtein, A.1    Karpol, A.2    Barak, Y.3    Lamed, R.4    Bayer, E.A.5
  • 7
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22(2):195- 201.
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 9
    • 80052962213 scopus 로고    scopus 로고
    • Kinetic partitioning mechanism governs the folding of the third FnIII domain of tenascin-C: Evidence at the single-molecule level
    • Peng Q, Fang J, Wang M, Li H (2011) Kinetic partitioning mechanism governs the folding of the third FnIII domain of tenascin-C: Evidence at the single-molecule level. J Mol Biol 412(4):698-709.
    • (2011) J Mol Biol , vol.412 , Issue.4 , pp. 698-709
    • Peng, Q.1    Fang, J.2    Wang, M.3    Li, H.4
  • 10
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276(5315):1109-1112. (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 11
    • 69549122277 scopus 로고    scopus 로고
    • On the remarkable mechanostability of scaffoldins and the mechanical clamp motif
    • Valbuena A, et al. (2009) On the remarkable mechanostability of scaffoldins and the mechanical clamp motif. Proc Natl Acad Sci USA 106(33):13791-13796.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.33 , pp. 13791-13796
    • Valbuena, A.1
  • 12
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: Probing proteins with AFM-based force spectroscopy
    • Puchner EM, Gaub HE (2009) Force and function: Probing proteins with AFM-based force spectroscopy. Curr Opin Struct Biol 19(5):605-614.
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.5 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 13
    • 77953231020 scopus 로고    scopus 로고
    • The folding cooperativity of a protein is controlled by its chain topology
    • Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C (2010) The folding cooperativity of a protein is controlled by its chain topology. Nature 465(7298):637-640.
    • (2010) Nature , vol.465 , Issue.7298 , pp. 637-640
    • Shank, E.A.1    Cecconi, C.2    Dill, J.W.3    Marqusee, S.4    Bustamante, C.5
  • 16
    • 77952358320 scopus 로고    scopus 로고
    • A "force buffer" protecting immunoglobulin titin
    • Nunes JM, et al. (2010) A "force buffer" protecting immunoglobulin titin. Angew Chem Int Ed Engl 49(20):3528-3531.
    • (2010) Angew Chem Int Ed Engl , vol.49 , Issue.20 , pp. 3528-3531
    • Nunes, J.M.1
  • 17
    • 76249114882 scopus 로고    scopus 로고
    • Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules
    • Puchner EM, Gaub HE (2010) Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules. Angew Chem Int Ed Engl 49(6):1147-1150.
    • (2010) Angew Chem Int Ed Engl , vol.49 , Issue.6 , pp. 1147-1150
    • Puchner, E.M.1    Gaub, H.E.2
  • 19
    • 33646587736 scopus 로고    scopus 로고
    • Nanomechanical measurements of the sequence-dependent folding landscapes of single nucleic acid hairpins
    • Woodside MT, et al. (2006) Nanomechanical measurements of the sequence-dependent folding landscapes of single nucleic acid hairpins. Proc Natl Acad Sci USA 103(16):6190-6195.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.16 , pp. 6190-6195
    • Woodside, M.T.1
  • 20
    • 46749112650 scopus 로고    scopus 로고
    • Comparing proteins by their unfolding pattern
    • Puchner EM, Franzen G, Gautel M, Gaub HE (2008) Comparing proteins by their unfolding pattern. Biophys J 95(1):426-434.
    • (2008) Biophys J , vol.95 , Issue.1 , pp. 426-434
    • Puchner, E.M.1    Franzen, G.2    Gautel, M.3    Gaub, H.E.4
  • 21
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • Rief M, Gautel M, Schemmel A, Gaub HE (1998) The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. Biophys J 75(6):3008-3014. (Pubitemid 28548968)
    • (1998) Biophysical Journal , vol.75 , Issue.6 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 24
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • DOI 10.1038/16219
    • Merkel R, Nassoy P, Leung A, Ritchie K, Evans E (1999) Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397(6714):50-53. (Pubitemid 29038244)
    • (1999) Nature , vol.397 , Issue.6714 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 25
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E, Ritchie K (1997) Dynamic strength of molecular adhesion bonds. Biophys J 72(4):1541-1555. (Pubitemid 27133095)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 26
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell GI (1978) Models for the specific adhesion of cells to cells. Science 200(4342):618-627.
    • (1978) Science , vol.200 , Issue.4342 , pp. 618-627
    • Bell, G.I.1
  • 28
    • 0034702770 scopus 로고    scopus 로고
    • Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy
    • DOI 10.1021/bi992715o
    • Yuan C, Chen A, Kolb P, Moy VT (2000) Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. Biochemistry 39(33):10219-10223. (Pubitemid 30663044)
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10219-10223
    • Yuan, C.1    Chen, A.2    Kolb, P.3    Moy, V.T.4
  • 29
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy VT, Florin EL, Gaub HE (1994) Intermolecular forces and energies between ligands and receptors. Science 266(5183):257-259. (Pubitemid 24343509)
    • (1994) Science , vol.266 , Issue.5183 , pp. 257-259
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 30
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin EL, Moy VT, Gaub HE (1994) Adhesion forces between individual ligand-receptor pairs. Science 264(5157):415-417. (Pubitemid 24179839)
    • (1994) Science , vol.264 , Issue.5157 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 31
    • 4143061576 scopus 로고    scopus 로고
    • Cohesin-dockerin interaction in cellulosome assembly: A single Asp-to-Asn mutation disrupts high-affinity cohesin-dockerin binding
    • DOI 10.1016/j.febslet.2004.07.040, PII S0014579304009081
    • Handelsman T, et al. (2004) Cohesin-dockerin interaction in cellulosome assembly: A single Asp-to-Asn mutation disrupts high-affinity cohesin-dockerin binding. FEBS Lett 572(1-3):195-200. (Pubitemid 39092535)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 195-200
    • Handelsman, T.1    Barak, Y.2    Nakar, D.3    Mechaly, A.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 32
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single calmodulin molecules
    • Junker JP, Ziegler F, Rief M (2009) Ligand-dependent equilibrium fluctuations of single calmodulin molecules. Science 323(5914):633-637.
    • (2009) Science , vol.323 , Issue.5914 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 33
    • 0036106315 scopus 로고    scopus 로고
    • Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy
    • Desmeules P, Grandbois M, Bondarenko VA, Yamazaki A, Salesse C (2002) Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy. Biophys J 82(6):3343-3350. (Pubitemid 34547676)
    • (2002) Biophysical Journal , vol.82 , Issue.6 , pp. 3343-3350
    • Desmeules, P.1    Grandbois, M.2    Bondarenko, V.A.3    Yamazaki, A.4    Salesse, C.5
  • 34
    • 45849108388 scopus 로고    scopus 로고
    • Biochemistry. How enzymes work
    • Ringe D, Petsko GA (2008) Biochemistry. How enzymes work. Science 320(5882):1428-1429.
    • (2008) Science , vol.320 , Issue.5882 , pp. 1428-1429
    • Ringe, D.1    Petsko, G.A.2
  • 35
    • 51649101588 scopus 로고    scopus 로고
    • Mechanoenzymatics of titin kinase
    • Puchner EM, et al. (2008) Mechanoenzymatics of titin kinase. Proc Natl Acad Sci USA 105(36):13385-13390.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.36 , pp. 13385-13390
    • Puchner, E.M.1
  • 36
    • 70349961707 scopus 로고    scopus 로고
    • Triggering enzymatic activity with force
    • Gumpp H, et al. (2009) Triggering enzymatic activity with force. Nano Lett 9(9):3290-3295.
    • (2009) Nano Lett , vol.9 , Issue.9 , pp. 3290-3295
    • Gumpp, H.1
  • 38
    • 69449083856 scopus 로고    scopus 로고
    • The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk
    • Bertz M, Wilmanns M, Rief M (2009) The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk. Proc Natl Acad Sci USA 106(32): 13307-13310.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.32 , pp. 13307-13310
    • Bertz, M.1    Wilmanns, M.2    Rief, M.3
  • 39
    • 77952176659 scopus 로고    scopus 로고
    • Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments
    • Zimmermann JL, Nicolaus T, Neuert G, Blank K (2010) Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments. Nat Protoc 5(6):975-985.
    • (2010) Nat Protoc , vol.5 , Issue.6 , pp. 975-985
    • Zimmermann, J.L.1    Nicolaus, T.2    Neuert, G.3    Blank, K.4
  • 40
    • 33646192726 scopus 로고    scopus 로고
    • Practical implementation of dynamic methods for measuring atomic force microscope cantilever spring constants
    • Cook S, et al. (2006) Practical implementation of dynamic methods for measuring atomic force microscope cantilever spring constants. Nanotechnology 17(9):2135-2145.
    • (2006) Nanotechnology , vol.17 , Issue.9 , pp. 2135-2145
    • Cook, S.1
  • 41
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic-force microscopy
    • Butt HJ, Jaschke M (1995) Calculation of thermal noise in atomic-force microscopy. Nanotechnology 6(1):1-7.
    • (1995) Nanotechnology , vol.6 , Issue.1 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.