메뉴 건너뛰기




Volumn 406, Issue 3, 2011, Pages 362-370

M13 procoat protein insertion into YidC and SecYEG proteoliposomes and liposomes

Author keywords

electrochemical membrane potential; membrane insertion; protein translocation; Sec translocase; YidC insertase

Indexed keywords

CARRIER PROTEIN; ENZYME PRECURSOR; LIPOSOME; M13 PROCOAT PROTEIN; MEMBRANE ENZYME; MEMBRANE INSERTASE; MEMBRANE PROTEIN; MUTANT PROTEIN; PERIPLASMIC PROTEIN; PROTEIN H5EE; PROTEIN SECYEG; PROTEIN YIDC; UNCLASSIFIED DRUG;

EID: 79551687349     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.12.036     Document Type: Article
Times cited : (26)

References (34)
  • 1
    • 0019330536 scopus 로고
    • Assembly of proteins into membranes
    • Wickner W.T. Assembly of proteins into membranes Science 210 1980 861 868
    • (1980) Science , vol.210 , pp. 861-868
    • Wickner, W.T.1
  • 2
    • 0025142363 scopus 로고
    • Initial steps in protein membrane insertion. Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction
    • Gallusser A., and Kuhn A. Initial steps in protein membrane insertion. Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction EMBO J. 9 1990 2723 2729
    • (1990) EMBO J. , vol.9 , pp. 2723-2729
    • Gallusser, A.1    Kuhn, A.2
  • 3
    • 0023054119 scopus 로고
    • Both hydrophobic domains of M13 procoat initiate membrane insertion
    • Kuhn A., Kreil G., and Wickner W. Both hydrophobic domains of M13 procoat initiate membrane insertion EMBO J. 5 1986 3681 3685
    • (1986) EMBO J. , vol.5 , pp. 3681-3685
    • Kuhn, A.1    Kreil, G.2    Wickner, W.3
  • 4
    • 0035860693 scopus 로고    scopus 로고
    • Function of YidC for the insertion of M13 procoat protein in E. coli: Translocation of mutants that show differences in their membrane potential dependence and Sec-requirement
    • Samuelson J.C., Jiang F., Yi L., Chen M., Kuhn A., and Dalbey R.E. Function of YidC for the insertion of M13 procoat protein in E. coli: translocation of mutants that show differences in their membrane potential dependence and Sec-requirement J. Biol. Chem. 276 2001 34847 34852
    • (2001) J. Biol. Chem. , vol.276 , pp. 34847-34852
    • Samuelson, J.C.1    Jiang, F.2    Yi, L.3    Chen, M.4    Kuhn, A.5    Dalbey, R.E.6
  • 5
    • 0022654552 scopus 로고
    • The cytoplasmic carboxy-terminus is required for the membrane insertion of the central domain of M13 procoat
    • Kuhn A., Wickner W., and Kreil G. The cytoplasmic carboxy-terminus is required for the membrane insertion of the central domain of M13 procoat Nature 322 1986 335 339
    • (1986) Nature , vol.322 , pp. 335-339
    • Kuhn, A.1    Wickner, W.2    Kreil, G.3
  • 6
    • 0019420801 scopus 로고
    • Membrane assembly from purified components: II. Assembly of M13 procoat into liposomes reconstituted with purified leader peptidase
    • Watts C., Silver P., and Wickner W. Membrane assembly from purified components: II. Assembly of M13 procoat into liposomes reconstituted with purified leader peptidase Cell 25 1981 347 353
    • (1981) Cell , vol.25 , pp. 347-353
    • Watts, C.1    Silver, P.2    Wickner, W.3
  • 7
    • 0021099109 scopus 로고
    • Reconstitution of rapid and asymmetric assembly of M13 procoat protein into liposomes which have bacterial leader peptidase
    • Ohno-Iwashita Y., and Wickner W. Reconstitution of rapid and asymmetric assembly of M13 procoat protein into liposomes which have bacterial leader peptidase J. Biol. Chem. 258 1983 1895 1900
    • (1983) J. Biol. Chem. , vol.258 , pp. 1895-1900
    • Ohno-Iwashita, Y.1    Wickner, W.2
  • 8
    • 0022400507 scopus 로고
    • Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane
    • Dalbey R.E., and Wickner W. Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane J. Biol. Chem. 260 1985 15925 15931
    • (1985) J. Biol. Chem. , vol.260 , pp. 15925-15931
    • Dalbey, R.E.1    Wickner, W.2
  • 9
    • 0022398528 scopus 로고
    • M13 procoat inserts into liposomes in the absence of other membrane proteins
    • Geller B.L., and Wickner W. M13 procoat inserts into liposomes in the absence of other membrane proteins J. Biol. Chem. 260 1985 13281 13285
    • (1985) J. Biol. Chem. , vol.260 , pp. 13281-13285
    • Geller, B.L.1    Wickner, W.2
  • 10
    • 33846012223 scopus 로고    scopus 로고
    • A derivative of lipid A is involved in signal recognition particle/SecYEG-dependent and -independent membrane integrations
    • Nishiyama K., Ikegami A., Moser M., Schlitz E., Tokuda H., and Müller M. A derivative of lipid A is involved in signal recognition particle/SecYEG-dependent and -independent membrane integrations J. Biol. Chem. 281 2006 35667 35676
    • (2006) J. Biol. Chem. , vol.281 , pp. 35667-35676
    • Nishiyama, K.1    Ikegami, A.2    Moser, M.3    Schlitz, E.4    Tokuda, H.5    Müller, M.6
  • 11
    • 54049123018 scopus 로고    scopus 로고
    • Diacylglycerol specifically blocks spontaneous integration of membrane proteins and allows detection of a factor-assisted integration
    • Kawashima Y., Miyazaki E., Müller M., Tokuda H., and Nishiyama K. Diacylglycerol specifically blocks spontaneous integration of membrane proteins and allows detection of a factor-assisted integration J. Biol. Chem. 283 2008 24489 25596
    • (2008) J. Biol. Chem. , vol.283 , pp. 24489-25596
    • Kawashima, Y.1    Miyazaki, E.2    Müller, M.3    Tokuda, H.4    Nishiyama, K.5
  • 12
    • 78649764518 scopus 로고    scopus 로고
    • Coupled cell-free synthesis and lipid vesicle insertion of a functional oligomeric channel MscL
    • Berrier C., Guilvout I., Bayan N., Park K.H., Mesneau A., and Chami M. Coupled cell-free synthesis and lipid vesicle insertion of a functional oligomeric channel MscL Biochem. Biophys. Acta 1808 2010 41 46
    • (2010) Biochem. Biophys. Acta , vol.1808 , pp. 41-46
    • Berrier, C.1    Guilvout, I.2    Bayan, N.3    Park, K.H.4    Mesneau, A.5    Chami, M.6
  • 13
    • 0034632819 scopus 로고    scopus 로고
    • YidC mediates both Sec-dependent and Sec-independent membrane protein insertion
    • Samuelson J.C., Chen M., Jiang F., Möller I., Wiedmann M., and Kuhn A. YidC mediates both Sec-dependent and Sec-independent membrane protein insertion Nature 406 2000 637 641
    • (2000) Nature , vol.406 , pp. 637-641
    • Samuelson, J.C.1    Chen, M.2    Jiang, F.3    Möller, I.4    Wiedmann, M.5    Kuhn, A.6
  • 14
    • 0347157958 scopus 로고    scopus 로고
    • A new family of proteins catalyzes the membrane insertion process of proteins
    • Kuhn A., Stuart R., Henry R., and Dalbey R. A new family of proteins catalyzes the membrane insertion process of proteins Trends Cell Biol. 13 2003 510 516
    • (2003) Trends Cell Biol. , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.4
  • 15
    • 1542676909 scopus 로고    scopus 로고
    • Defining the regions of Escherichia coli YidC that contribute to activity
    • Jiang F., Chen M., Yi L., de Gier J.W., Kuhn A., and Dalbey R.E. Defining the regions of Escherichia coli YidC that contribute to activity J. Biol. Chem. 278 2003 48965 48972
    • (2003) J. Biol. Chem. , vol.278 , pp. 48965-48972
    • Jiang, F.1    Chen, M.2    Yi, L.3    De Gier, J.W.4    Kuhn, A.5    Dalbey, R.E.6
  • 18
    • 0022343605 scopus 로고
    • Conserved residues of the leader peptide are essential for cleavage by leader peptidase
    • Kuhn A., and Wickner W. Conserved residues of the leader peptide are essential for cleavage by leader peptidase J. Biol. Chem. 260 1985 15914 15918
    • (1985) J. Biol. Chem. , vol.260 , pp. 15914-15918
    • Kuhn, A.1    Wickner, W.2
  • 20
    • 0025277448 scopus 로고
    • Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion
    • 2429
    • Kuhn, A., Zhu, H. Y. & Dalbey, R. E. (1990) Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion. EMBO J. 9, 2385-2388, 2429.
    • (1990) EMBO J. , vol.9 , pp. 2385-2388
    • Kuhn, A.1    Zhu, H.Y.2    Dalbey, R.E.3
  • 21
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential-evidence for an electrophoresis-like membrane transfer mechanism
    • Cao G., Kuhn A., and Dalbey R.E. The translocation of negatively charged residues across the membrane is driven by the electrochemical potential-evidence for an electrophoresis-like membrane transfer mechanism EMBO J. 14 1995 866 875
    • (1995) EMBO J. , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.E.3
  • 22
    • 0035851183 scopus 로고    scopus 로고
    • Indecisive M13 procoat mutants bind to SecA but do not activate the translocation ATPase
    • Roos T., Kiefer D., Hugenschmidt S., Economou A., and Kuhn A. Indecisive M13 procoat mutants bind to SecA but do not activate the translocation ATPase J. Biol. Chem. 276 2001 37909 37915
    • (2001) J. Biol. Chem. , vol.276 , pp. 37909-37915
    • Roos, T.1    Kiefer, D.2    Hugenschmidt, S.3    Economou, A.4    Kuhn, A.5
  • 23
    • 85047694884 scopus 로고
    • Alterations in the extracellular domain of M13 procoat make its membrane insertion dependent on secA and secY
    • Kuhn A. Alterations in the extracellular domain of M13 procoat make its membrane insertion dependent on secA and secY Eur. J. Biochem. 177 1988 267 271
    • (1988) Eur. J. Biochem. , vol.177 , pp. 267-271
    • Kuhn, A.1
  • 25
    • 2142705713 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
    • van der Laan M., Bechtluft P., Kol S., Nouwen N., and Driessen A.J. F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis J. Cell Biol. 165 2004 213 222
    • (2004) J. Cell Biol. , vol.165 , pp. 213-222
    • Van Der Laan, M.1    Bechtluft, P.2    Kol, S.3    Nouwen, N.4    Driessen, A.J.5
  • 26
    • 33845761509 scopus 로고    scopus 로고
    • The mechanosensitive channel protein MscL is targeted by SRP to the novel YidC membrane insertion pathway of E. coli
    • Facey S., Neugebauer S., Krauss S., and Kuhn A. The mechanosensitive channel protein MscL is targeted by SRP to the novel YidC membrane insertion pathway of E. coli J. Mol. Biol. 385 2007 995 1004
    • (2007) J. Mol. Biol. , vol.385 , pp. 995-1004
    • Facey, S.1    Neugebauer, S.2    Krauss, S.3    Kuhn, A.4
  • 27
    • 0020479149 scopus 로고
    • The biosynthesis of membrane-bound M13 coat protein. Energetics and assembly intermediates
    • Zimmermann R., Watts C., and Wickner W. The biosynthesis of membrane-bound M13 coat protein. Energetics and assembly intermediates J. Biol. Chem. 257 1982 6529 6536
    • (1982) J. Biol. Chem. , vol.257 , pp. 6529-6536
    • Zimmermann, R.1    Watts, C.2    Wickner, W.3
  • 28
    • 0033548545 scopus 로고    scopus 로고
    • Direct evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins
    • Schuenemann T.A., Delgado-Nixon V.M., and Dalbey R.E. Direct evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins J Biol. Chem. 274 1999 6855 6864
    • (1999) J Biol. Chem. , vol.274 , pp. 6855-6864
    • Schuenemann, T.A.1    Delgado-Nixon, V.M.2    Dalbey, R.E.3
  • 29
    • 0037040894 scopus 로고    scopus 로고
    • Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane insertion
    • Chen M., Samuelson J., Jiang F., Müller M., Kuhn A., and Dalbey R.E. Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane insertion J. Biol. Chem. 277 2002 7670 7675
    • (2002) J. Biol. Chem. , vol.277 , pp. 7670-7675
    • Chen, M.1    Samuelson, J.2    Jiang, F.3    Müller, M.4    Kuhn, A.5    Dalbey, R.E.6
  • 30
    • 0033428711 scopus 로고    scopus 로고
    • A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
    • Karamanou S., Vrontou E., Sianidis G., Baud C., Roos T., and Kuhn A. A molecular switch in SecA protein couples ATP hydrolysis to protein translocation Mol. Microbiol. 34 1999 1133 1145
    • (1999) Mol. Microbiol. , vol.34 , pp. 1133-1145
    • Karamanou, S.1    Vrontou, E.2    Sianidis, G.3    Baud, C.4    Roos, T.5    Kuhn, A.6
  • 31
    • 0035873223 scopus 로고    scopus 로고
    • Projection structure and oligomeric properties of a bacterial core protein translocase
    • Collinson I., Breyton C., Duong F., Tziatzios C., Schubert D., and Or E. Projection structure and oligomeric properties of a bacterial core protein translocase EMBO J. 20 2001 2462 2471
    • (2001) EMBO J. , vol.20 , pp. 2462-2471
    • Collinson, I.1    Breyton, C.2    Duong, F.3    Tziatzios, C.4    Schubert, D.5    Or, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.