메뉴 건너뛰기




Volumn 105, Issue 11, 2008, Pages 4127-4132

Contribution of positively charged flanking residues to the insertion of transmembrane helices into the endoplasmic reticulum

Author keywords

Hydrophobicity scale; Membrane protein; Positive inside rule; Translocon

Indexed keywords

AMINO ACID; ARGININE; LYSINE; CATION; ESCHERICHIA COLI PROTEIN;

EID: 41949125627     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0711580105     Document Type: Article
Times cited : (56)

References (26)
  • 1
    • 2542452829 scopus 로고    scopus 로고
    • Cotranslational membrane protein biogenesis at the endoplasmic reticulum
    • Alder NN, Johnson AE (2004) Cotranslational membrane protein biogenesis at the endoplasmic reticulum. J Biol Chem 279:22787-22790.
    • (2004) J Biol Chem , vol.279 , pp. 22787-22790
    • Alder, N.N.1    Johnson, A.E.2
  • 2
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport TA (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450:663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 3
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T, et al. (2005) Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433:377-381.
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1
  • 4
    • 20044389842 scopus 로고    scopus 로고
    • Membrane insertion of a potassium channel voltage sensor
    • Hessa T, White SH, von Heijne G (2005) Membrane insertion of a potassium channel voltage sensor. Science 307:1427.
    • (2005) Science , vol.307 , pp. 1427
    • Hessa, T.1    White, S.H.2    von Heijne, G.3
  • 5
    • 33750498869 scopus 로고    scopus 로고
    • Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly
    • Meindl-Beinker NM, Lundin C, Nilsson I, White SH, von Heijne G (2006) Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly. EMBO Rep 7:1111-1116.
    • (2006) EMBO Rep , vol.7 , pp. 1111-1116
    • Meindl-Beinker, N.M.1    Lundin, C.2    Nilsson, I.3    White, S.H.4    von Heijne, G.5
  • 6
    • 37249037182 scopus 로고    scopus 로고
    • Molecular code for transmembrane-helix recognition by the Sec61 translocon
    • Hessa T, et al. (2007) Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 450:1026-1030.
    • (2007) Nature , vol.450 , pp. 1026-1030
    • Hessa, T.1
  • 7
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley WC, Creamer TP, White SH (1996) Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry 35:5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 8
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: Derivation of an implicit membrane potential
    • Ulmschneider MB, Sansom MS, Di Nola (2005) Properties of integral membrane protein structures: Derivation of an implicit membrane potential. Proteins 59:252-265.
    • (2005) Proteins , vol.59 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.2    Nola, D.3
  • 9
    • 0347192985 scopus 로고    scopus 로고
    • X-ray structure of a protein-conducting channel
    • van den Berg B, et al. (2004) X-ray structure of a protein-conducting channel. Nature 427:36-44.
    • (2004) Nature , vol.427 , pp. 36-44
    • van den Berg, B.1
  • 10
    • 34248523155 scopus 로고    scopus 로고
    • The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal
    • Li W, et al. (2007) The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal. Mol Cell 26:511-521.
    • (2007) Mol Cell , vol.26 , pp. 511-521
    • Li, W.1
  • 11
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy M, Junne T, Spiess M (2004) Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43:12716-12722.
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 12
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • von Heijne G (1986) The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J 5:3021-3027.
    • (1986) EMBO J , vol.5 , pp. 3021-3027
    • von Heijne, G.1
  • 13
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G (1989) Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • von Heijne, G.1
  • 14
    • 0023036920 scopus 로고
    • Net N-C charge imbalance may be important for signal sequence function in bacteria
    • von Heijne G (1986) Net N-C charge imbalance may be important for signal sequence function in bacteria. J Mol Biol 192:287-290.
    • (1986) J Mol Biol , vol.192 , pp. 287-290
    • von Heijne, G.1
  • 15
    • 0014050060 scopus 로고
    • Sequence analysis of melittin from tryptic and peptic degradation products
    • Habermann E, Jentsch J (1967) Sequence analysis of melittin from tryptic and peptic degradation products. Hoppe Seylers Z Physiol Chem 348:37-50.
    • (1967) Hoppe Seylers Z Physiol Chem , vol.348 , pp. 37-50
    • Habermann, E.1    Jentsch, J.2
  • 16
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • Sitaram N, Nagaraj R (1999) Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity. Biochim Biophys Acta 1462:29-54.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 17
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger B, Lohner K (2006) Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim Biophys Acta 1758:1529-1539.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 18
    • 0032006057 scopus 로고    scopus 로고
    • Stop-transfer function of pseudo-random amino acid segments during translocation across prokaryotic and eukaryotic membranes
    • Sääf A, Wallin E, von Heijne G (1998) Stop-transfer function of pseudo-random amino acid segments during translocation across prokaryotic and eukaryotic membranes. Eur J Biochem 251:821-829.
    • (1998) Eur J Biochem , vol.251 , pp. 821-829
    • Sääf, A.1    Wallin, E.2    von Heijne, G.3
  • 19
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
    • Johansson M, Nilsson I, von Heijne G (1993) Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol Gen Genet 239:251-256.
    • (1993) Mol Gen Genet , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    von Heijne, G.3
  • 20
    • 0035843981 scopus 로고    scopus 로고
    • Effects of "hydrophobic mismatch" on the location of transmembrane helices in the ER membrane
    • Monné M, von Heijne G (2001) Effects of "hydrophobic mismatch" on the location of transmembrane helices in the ER membrane. FEBS Lett 496:96-100.
    • (2001) FEBS Lett , vol.496 , pp. 96-100
    • Monné, M.1    von Heijne, G.2
  • 21
    • 2342544065 scopus 로고    scopus 로고
    • Snorkeling preferences foster an amino acid composition bias in transmembrane helices
    • Chamberlain AK, Lee Y, Kim S, Bowie JU (2004) Snorkeling preferences foster an amino acid composition bias in transmembrane helices. J Mol Biol 339:471-479.
    • (2004) J Mol Biol , vol.339 , pp. 471-479
    • Chamberlain, A.K.1    Lee, Y.2    Kim, S.3    Bowie, J.U.4
  • 22
    • 12344330612 scopus 로고    scopus 로고
    • A study of the membrane-water interface region of membrane proteins
    • Granseth E, von Heijne G, Elofsson A (2005) A study of the membrane-water interface region of membrane proteins. J Mol Biol 346:377-385.
    • (2005) J Mol Biol , vol.346 , pp. 377-385
    • Granseth, E.1    von Heijne, G.2    Elofsson, A.3
  • 23
    • 33644855546 scopus 로고    scopus 로고
    • Function of positive charges following signal-anchor sequences during translocation of the N-terminal domain
    • Kida Y, Morimoto F, Mihara K, Sakaguchi M (2006) Function of positive charges following signal-anchor sequences during translocation of the N-terminal domain. J Biol Chem 281:1152-1158.
    • (2006) J Biol Chem , vol.281 , pp. 1152-1158
    • Kida, Y.1    Morimoto, F.2    Mihara, K.3    Sakaguchi, M.4
  • 24
    • 0035834515 scopus 로고    scopus 로고
    • Formation of helical hairpins during membrane protein integration into the endoplasmic reticulum membrane: Role of the N, C-terminal flanking regions
    • Hermansson M, Monné M, von Heijne G (2001) Formation of helical hairpins during membrane protein integration into the endoplasmic reticulum membrane: Role of the N, C-terminal flanking regions. J Mol Biol 313:1171-1179.
    • (2001) J Mol Biol , vol.313 , pp. 1171-1179
    • Hermansson, M.1    Monné, M.2    von Heijne, G.3
  • 25
    • 1542313960 scopus 로고    scopus 로고
    • Sec61p contributes to signal sequence orientation according to the positive-inside rule
    • Goder V, Junne T, Spiess M (2004) Sec61p contributes to signal sequence orientation according to the positive-inside rule. Mol Biol Cell 15:1470-1478.
    • (2004) Mol Biol Cell , vol.15 , pp. 1470-1478
    • Goder, V.1    Junne, T.2    Spiess, M.3
  • 26
    • 36349034451 scopus 로고    scopus 로고
    • Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology
    • Junne T, Schwede T, Goder V, Spiess M (2007) Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. J Biol Chem 282:33201-33209.
    • (2007) J Biol Chem , vol.282 , pp. 33201-33209
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.