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Volumn 274, Issue 2, 2007, Pages 463-473

Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains

Author keywords

Expressed protein ligation; Helicase; Interdomain communication; RNA dependent ATPase

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE TRIPHOSPHATASE; RNA HELICASE;

EID: 33845967782     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05593.x     Document Type: Article
Times cited : (20)

References (31)
  • 2
    • 0024781056 scopus 로고
    • Protein sorting in yeast: The role of the vacuolar proton-translocating ATPase
    • Kane PM, Yamashiro CT, Rothman JH & Stevens TH (1989) Protein sorting in yeast: the role of the vacuolar proton-translocating ATPase. J Cell Sci Suppl 11, 161-178.
    • (1989) J Cell Sci Suppl , vol.11 , pp. 161-178
    • Kane, P.M.1    Yamashiro, C.T.2    Rothman, J.H.3    Stevens, T.H.4
  • 3
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus H (2000) Protein splicing and related forms of protein autoprocessing. Annu Rev Biochem 69, 447-496.
    • (2000) Annu Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 4
    • 1342301482 scopus 로고    scopus 로고
    • Expressed protein ligation. Method and applications
    • David R, Richter MP & Beck-Sickinger AG (2004) Expressed protein ligation. Method and applications. Eur J Biochem 271, 663-677.
    • (2004) Eur J Biochem , vol.271 , pp. 663-677
    • David, R.1    Richter, M.P.2    Beck-Sickinger, A.G.3
  • 5
    • 0036669566 scopus 로고    scopus 로고
    • Recent advances in the application of expressed protein ligation to protein engineering
    • Hofmann RM & Muir TW (2002) Recent advances in the application of expressed protein ligation to protein engineering. Curr Opin Biotechnol 13, 297-303.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 297-303
    • Hofmann, R.M.1    Muir, T.W.2
  • 6
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson PE, Muir TW, Clark-Lewis I & Kent SB (1994) Synthesis of proteins by native chemical ligation. Science 266, 776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 7
    • 0033582287 scopus 로고    scopus 로고
    • Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
    • Xu R, Ayers B, Cowburn D & Muir TW (1999) Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc Natl Acad Sci USA 96, 388-393.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 388-393
    • Xu, R.1    Ayers, B.2    Cowburn, D.3    Muir, T.W.4
  • 10
    • 0342470656 scopus 로고    scopus 로고
    • Intein-mediated protein ligation: Harnessing nature's escape artists
    • Evans TC Jr & Xu MQ (1999) Intein-mediated protein ligation: harnessing nature's escape artists. Biopolymers 51, 333-342.
    • (1999) Biopolymers , vol.51 , pp. 333-342
    • Evans Jr, T.C.1    Xu, M.Q.2
  • 11
    • 0033614484 scopus 로고    scopus 로고
    • Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: Facile production of protein building blocks for protein ligation
    • Mathys S, Evans TC, Chute IC, Wu H, Chong S, Benner J, Liu XQ & Xu MQ (1999) Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: facile production of protein building blocks for protein ligation. Gene 231, 1-13.
    • (1999) Gene , vol.231 , pp. 1-13
    • Mathys, S.1    Evans, T.C.2    Chute, I.C.3    Wu, H.4    Chong, S.5    Benner, J.6    Liu, X.Q.7    Xu, M.Q.8
  • 12
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O, Banroques J, Tanner NK & Linder P (2006) The DEAD-box protein family of RNA helicases. Gene 367, 17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 13
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya AE & Koonin EV (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr Opin Struct Biol 3, 419-429.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 14
    • 23644449094 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of DEAD-box protein Dhh1p
    • Cheng Z, Coller J, Parker R & Song H (2005) Crystal structure and functional analysis of DEAD-box protein Dhh1p. RNA 11, 1258-1270.
    • (2005) RNA , vol.11 , pp. 1258-1270
    • Cheng, Z.1    Coller, J.2    Parker, R.3    Song, H.4
  • 15
    • 0035852638 scopus 로고    scopus 로고
    • Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii
    • Story RM, Li H & Abelson JN (2001) Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc Natl Acad Sci USA 98, 1465-1470.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1465-1470
    • Story, R.M.1    Li, H.2    Abelson, J.N.3
  • 16
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers JM, Johnson ER & McKay DB (2000) Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci USA 97, 13080-13085.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 17
    • 11144222543 scopus 로고    scopus 로고
    • Crystal structure of the human ATP-dependent splicing and export factor UAP56
    • Shi H, Cordin O, Minder CM, Linder P & Xu RM (2004) Crystal structure of the human ATP-dependent splicing and export factor UAP56. Proc Natl Acad Sci USA 101, 17628-17633.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17628-17633
    • Shi, H.1    Cordin, O.2    Minder, C.M.3    Linder, P.4    Xu, R.M.5
  • 18
    • 4143076853 scopus 로고    scopus 로고
    • Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export
    • Zhao R, Shen J, Green MR, MacMorris M & Blumenthal T (2004) Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export. Structure 12, 1373-1381.
    • (2004) Structure , vol.12 , pp. 1373-1381
    • Zhao, R.1    Shen, J.2    Green, M.R.3    MacMorris, M.4    Blumenthal, T.5
  • 20
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C & Caron PR (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6, 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 21
    • 0033214805 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: Delineation of a novel sub-family of bacterial DEAD proteins
    • Kossen K & Uhlenbeck OC (1999) Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: delineation of a novel sub-family of bacterial DEAD proteins. Nucleic Acids Res 27, 3811-3820.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3811-3820
    • Kossen, K.1    Uhlenbeck, O.C.2
  • 22
    • 27444442034 scopus 로고    scopus 로고
    • YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain
    • Karginov FV, Caruthers JM, Hu Y, McKay DB & Uhlenbeck OC (2005) YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. J Biol Chem 280, 35499-35505.
    • (2005) J Biol Chem , vol.280 , pp. 35499-35505
    • Karginov, F.V.1    Caruthers, J.M.2    Hu, Y.3    McKay, D.B.4    Uhlenbeck, O.C.5
  • 23
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Bates PA, Kelley LA, MacCallum RM & Sternberg MJ (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins Supplement 5, 39-46.
    • (2001) Proteins Supplement , vol.5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 24
    • 33646017369 scopus 로고    scopus 로고
    • Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa
    • Sengoku T, Nureki O, Nakamura A, Kobayashi S & Yokoyama S (2006) Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa. Cell 125, 287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 25
    • 0028881551 scopus 로고
    • Secondary structure of RecA in solution. The effects of cofactor, DNA and ionic conditions
    • Wittung P, Norden B & Takahashi M (1995) Secondary structure of RecA in solution. The effects of cofactor, DNA and ionic conditions. Eur J Biochem 228, 149-154.
    • (1995) Eur J Biochem , vol.228 , pp. 149-154
    • Wittung, P.1    Norden, B.2    Takahashi, M.3
  • 27
    • 12344279980 scopus 로고    scopus 로고
    • Equilibrium and kinetic analysis of nucleotide binding to the DEAD-box RNA helicase DbpA
    • Talavera MA & De La Cruz EM (2005) Equilibrium and kinetic analysis of nucleotide binding to the DEAD-box RNA helicase DbpA. Biochemistry 44, 959-970.
    • (2005) Biochemistry , vol.44 , pp. 959-970
    • Talavera, M.A.1    De La Cruz, E.M.2
  • 28
    • 0036927393 scopus 로고    scopus 로고
    • The carboxy-terminal domain of the DExD/H protein YxiN is sufficient to confer specificity for 23S rRNA
    • Kossen K, Karginov FV & Uhlenbeck OC (2002) The carboxy-terminal domain of the DExD/H protein YxiN is sufficient to confer specificity for 23S rRNA. J Mol Biol 324, 625-636.
    • (2002) J Mol Biol , vol.324 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 29
    • 0032387820 scopus 로고    scopus 로고
    • Kinetic analysis of the RNA-dependent adenosinetriphosphatase activity of DbpA, an Escherichia coli DEAD protein specific for 23S ribosomal RNA
    • Tsu CA & Uhlenbeck OC (1998) Kinetic analysis of the RNA-dependent adenosinetriphosphatase activity of DbpA, an Escherichia coli DEAD protein specific for 23S ribosomal RNA. Biochemistry 37, 16989-16996.
    • (1998) Biochemistry , vol.37 , pp. 16989-16996
    • Tsu, C.A.1    Uhlenbeck, O.C.2
  • 30
    • 0037133527 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
    • Polach KJ & Uhlenbeck OC (2002) Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry 41, 3693-3702.
    • (2002) Biochemistry , vol.41 , pp. 3693-3702
    • Polach, K.J.1    Uhlenbeck, O.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.