메뉴 건너뛰기




Volumn 1818, Issue 12, 2012, Pages 3158-3166

Deletion of a single helix from the transmembrane domain causes large changes in membrane insertion properties and secondary structure of the bacterial conjugation protein TrwB

Author keywords

Conjugative coupling protein; Infrared spectroscopy; Membrane protein; Membrane protein orientation; Membrane protein reconstitution; Transmembrane domain

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL CONJUGATION PROTEIN TRWB; DETERGENT; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84866491678     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.08.015     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 33646059524 scopus 로고    scopus 로고
    • 1-ATPase-like molecular motor involved in DNA transport during bacterial conjugation
    • 1-ATPase-like molecular motor involved in DNA transport during bacterial conjugation Res. Microbiol. 157 2006 299 305
    • (2006) Res. Microbiol. , vol.157 , pp. 299-305
    • Cabezon, E.1    De La Cruz, F.2
  • 2
    • 0025125379 scopus 로고
    • General organization of the conjugal transfer genes of the IncW plasmid R388 and interactions between R388 and IncN and IncP plasmids
    • S. Bolland, M. Llosa, P. Avila, and F. de la Cruz General organization of the conjugal transfer genes of the IncW plasmid R388 and interactions between R388 and IncN and IncP plasmids J. Bacteriol. 172 1990 5795 5802
    • (1990) J. Bacteriol. , vol.172 , pp. 5795-5802
    • Bolland, S.1    Llosa, M.2    Avila, P.3    De La Cruz, F.4
  • 3
    • 0037195792 scopus 로고    scopus 로고
    • Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation
    • I. Hormaeche, I. Alkorta, F. Moro, J.M. Valpuesta, F.M. Goñi, and F. de la Cruz Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation J. Biol. Chem. 277 2002 46456 46462
    • (2002) J. Biol. Chem. , vol.277 , pp. 46456-46462
    • Hormaeche, I.1    Alkorta, I.2    Moro, F.3    Valpuesta, J.M.4    Goñi, F.M.5    De La Cruz, F.6
  • 4
    • 1642483698 scopus 로고    scopus 로고
    • Role of the transmembrane domain in the stability of TrwB, an integral protein involved in bacterial conjugation
    • I. Hormaeche, I. Iloro, J.L. Arrondo, F.M. Goñi, F. de la Cruz, and I. Alkorta Role of the transmembrane domain in the stability of TrwB, an integral protein involved in bacterial conjugation J. Biol. Chem. 279 2004 10955 10961
    • (2004) J. Biol. Chem. , vol.279 , pp. 10955-10961
    • Hormaeche, I.1    Iloro, I.2    Arrondo, J.L.3    Goñi, F.M.4    De La Cruz, F.5    Alkorta, I.6
  • 5
    • 33646586059 scopus 로고    scopus 로고
    • The transmembrane domain provides nucleotide binding specificity to the bacterial conjugation protein TrwB
    • I. Hormaeche, R.L. Segura, A.J. Vecino, F.M. Goñi, F. de la Cruz, and I. Alkorta The transmembrane domain provides nucleotide binding specificity to the bacterial conjugation protein TrwB FEBS Lett. 580 2006 3075 3082
    • (2006) FEBS Lett. , vol.580 , pp. 3075-3082
    • Hormaeche, I.1    Segura, R.L.2    Vecino, A.J.3    Goñi, F.M.4    De La Cruz, F.5    Alkorta, I.6
  • 8
    • 0028047404 scopus 로고
    • Genetic organization of the conjugal DNA processing region of the IncW plasmid R388
    • M. Llosa, S. Bolland, and F. de la Cruz Genetic organization of the conjugal DNA processing region of the IncW plasmid R388 J. Mol. Biol. 235 1994 448 464
    • (1994) J. Mol. Biol. , vol.235 , pp. 448-464
    • Llosa, M.1    Bolland, S.2    De La Cruz, F.3
  • 9
    • 0020002423 scopus 로고
    • 1-ATPase interacts with a membrane protein component of a proton channel
    • 1-ATPase interacts with a membrane protein component of a proton channel Nature 298 1982 867 869
    • (1982) Nature , vol.298 , pp. 867-869
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 10
    • 0029007928 scopus 로고
    • DNA processing reactions in bacterial conjugation
    • E. Lanka, and B.M. Wilkins DNA processing reactions in bacterial conjugation Annu. Rev. Biochem. 64 1995 141 169
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 141-169
    • Lanka, E.1    Wilkins, B.M.2
  • 11
    • 2442483942 scopus 로고    scopus 로고
    • Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation
    • E. Cabezón, J.I. Sastre, and F. de la Cruz Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation Mol. Gen. Genet. 254 1997 400 406
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 400-406
    • Cabezón, E.1    Sastre, J.I.2    De La Cruz, F.3
  • 12
    • 20444431234 scopus 로고    scopus 로고
    • TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase
    • I. Tato, S. Zunzunegui, F. de la Cruz, and E. Cabezon TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase Proc. Natl. Acad. Sci. U. S. A. 102 2005 8156 8161
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8156-8161
    • Tato, I.1    Zunzunegui, S.2    De La Cruz, F.3    Cabezon, E.4
  • 13
    • 34548489399 scopus 로고    scopus 로고
    • The ATPase activity of the DNA transporter TrwB is modulated by protein TrwA: Implications for a common assembly mechanism of DNA translocating motors
    • I. Tato, I. Matilla, I. Arechaga, S. Zunzunegui, F. de la Cruz, and E. Cabezon The ATPase activity of the DNA transporter TrwB is modulated by protein TrwA: implications for a common assembly mechanism of DNA translocating motors J. Biol. Chem. 282 2007 25569 25576
    • (2007) J. Biol. Chem. , vol.282 , pp. 25569-25576
    • Tato, I.1    Matilla, I.2    Arechaga, I.3    Zunzunegui, S.4    De La Cruz, F.5    Cabezon, E.6
  • 14
    • 34948866886 scopus 로고    scopus 로고
    • Osmosensing properties of the histidine protein kinase MtrB from Corynebacterium glutamicum
    • N. Möker, P. Reihlen, R. Krämer, and S. Morbach Osmosensing properties of the histidine protein kinase MtrB from Corynebacterium glutamicum J. Biol. Chem. 282 2007 27666 27677
    • (2007) J. Biol. Chem. , vol.282 , pp. 27666-27677
    • Möker, N.1    Reihlen, P.2    Krämer, R.3    Morbach, S.4
  • 15
    • 33846103401 scopus 로고    scopus 로고
    • Purification of soluble and active RaxH, a transmembrane histidine protein kinase from Xanthomonas oryzae pv. oryzae required for AvrXa21 activity
    • A. Stolov, A. Valverde, P. Ronald, and S. Burdman Purification of soluble and active RaxH, a transmembrane histidine protein kinase from Xanthomonas oryzae pv. oryzae required for AvrXa21 activity Mol. Plant. Pathol. 8 2007 93 101
    • (2007) Mol. Plant. Pathol. , vol.8 , pp. 93-101
    • Stolov, A.1    Valverde, A.2    Ronald, P.3    Burdman, S.4
  • 17
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • M.J. Hope, M.B. Bally, G. Webb, and P.R. Cullis Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential Biochim. Biophys. Acta 812 1985 55 65
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0022348630 scopus 로고
    • Characterization of the solubilization of lipid bilayers by surfactants
    • D. Lichtenberg Characterization of the solubilization of lipid bilayers by surfactants Biochim. Biophys. Acta 821 1985 470 478
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 470-478
    • Lichtenberg, D.1
  • 21
    • 0015836627 scopus 로고
    • A simple procedure for removal of Triton X-100 from protein samples
    • P.W. Holloway A simple procedure for removal of Triton X-100 from protein samples Anal. Biochem. 53 1973 304 308
    • (1973) Anal. Biochem. , vol.53 , pp. 304-308
    • Holloway, P.W.1
  • 22
    • 50549164858 scopus 로고
    • A rapid and sensitive submicro phosphorus determination
    • C.S.F. Böttcher, C.M. Van Gent, and C. Fries A rapid and sensitive submicro phosphorus determination Anal. Chim. Acta 24 1961 203 204
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Böttcher, C.S.F.1    Van Gent, C.M.2    Fries, C.3
  • 23
    • 25844494293 scopus 로고    scopus 로고
    • Functional reconstitution of the Salmonella typhimurium PhoQ histidine kinase sensor in proteoliposomes
    • S. Sanowar, and H. Le Moual Functional reconstitution of the Salmonella typhimurium PhoQ histidine kinase sensor in proteoliposomes Biochem. J. 390 2005 769 776
    • (2005) Biochem. J. , vol.390 , pp. 769-776
    • Sanowar, S.1    Le Moual, H.2
  • 24
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • J.L. Arrondo, A. Muga, J. Castresana, and F.M. Goñi Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy Prog. Biophys. Mol. Biol. 59 1993 23 56
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 25
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • J.L. Arrondo, and F.M. Goñi Structure and dynamics of membrane proteins as studied by infrared spectroscopy Prog. Biophys. Mol. Biol. 72 1999 367 405
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.1    Goñi, F.M.2
  • 26
    • 0028295950 scopus 로고
    • Adaptation to altered growth temperatures in Acholeplasma laidlawii B: Fourier transform infrared studies of acyl chain conformational order in live cells
    • D.J. Moore, and R. Mendelsohn Adaptation to altered growth temperatures in Acholeplasma laidlawii B: Fourier transform infrared studies of acyl chain conformational order in live cells Biochemistry 33 1994 4080 4085
    • (1994) Biochemistry , vol.33 , pp. 4080-4085
    • Moore, D.J.1    Mendelsohn, R.2
  • 27
    • 0024291319 scopus 로고
    • Fourier transform infrared spectroscopy of 13CO-labeled phospholipids hydrogen bonding to carbonyl groups
    • A. Blume, W. Hübner, and G. Messner Fourier transform infrared spectroscopy of 13CO-labeled phospholipids hydrogen bonding to carbonyl groups Biochemistry 27 1988 8239 8249
    • (1988) Biochemistry , vol.27 , pp. 8239-8249
    • Blume, A.1    Hübner, W.2    Messner, G.3
  • 28
    • 0027298811 scopus 로고
    • Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy
    • E. Goormaghtigh, V. Cabiaux, J. De Meutter, M. Rosseneu, and J.M. Ruysschaert Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy Biochemistry 32 1993 6104 6110
    • (1993) Biochemistry , vol.32 , pp. 6104-6110
    • Goormaghtigh, E.1    Cabiaux, V.2    De Meutter, J.3    Rosseneu, M.4    Ruysschaert, J.M.5
  • 29
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • L.K. Tamm, and S.A. Tatulian Infrared spectroscopy of proteins and peptides in lipid bilayers Q. Rev. Biophys. 30 1997 365 429
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 31
    • 18044377435 scopus 로고    scopus 로고
    • Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein
    • N.M. Hooper Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein Biochem. Soc. Trans. 33 2005 335 338
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 335-338
    • Hooper, N.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.