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Volumn 426, Issue 1, 2014, Pages 185-198

Transmembrane segments form tertiary hairpins in the folding vestibule of the ribosome

Author keywords

folding of nascent peptides; intramolecular crosslinking; PEG MAL; potassium channel voltage sensor biogenesis; transmembrane helical hairpin

Indexed keywords

RIBOSOME PROTEIN; S3B HAIRPIN; S4 HAIRPIN; TRANSLOCON; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; CELL MEMBRANE PROTEIN; PROTEIN S6; S1 PROTEIN; S2 PROTEIN; S3 PROTEIN; S3B PROTEIN; S4 PROTEIN; S5 PROTEIN;

EID: 84890856922     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.09.013     Document Type: Article
Times cited : (48)

References (53)
  • 1
    • 79953106751 scopus 로고    scopus 로고
    • The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
    • D.N. Wilson, and R. Beckmann The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling Curr Opin Struct Biol 21 2011 274 282
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 274-282
    • Wilson, D.N.1    Beckmann, R.2
  • 2
    • 79960702711 scopus 로고    scopus 로고
    • Nascent peptide side chains induce rearrangements in distinct locations of the ribosomal tunnel
    • J. Lu, Z. Hua, W.R. Kobertz, and C. Deutsch Nascent peptide side chains induce rearrangements in distinct locations of the ribosomal tunnel J Mol Biol 411 2011 499 510
    • (2011) J Mol Biol , vol.411 , pp. 499-510
    • Lu, J.1    Hua, Z.2    Kobertz, W.R.3    Deutsch, C.4
  • 3
    • 77649273304 scopus 로고    scopus 로고
    • A folding zone in the ribosomal exit tunnel for Kv1.3 helix formation
    • L.W. Tu, and C. Deutsch A folding zone in the ribosomal exit tunnel for Kv1.3 helix formation J Mol Biol 396 2010 1346 1360
    • (2010) J Mol Biol , vol.396 , pp. 1346-1360
    • Tu, L.W.1    Deutsch, C.2
  • 5
    • 50849086415 scopus 로고    scopus 로고
    • Large-scale movement within the voltage-sensor paddle of a potassium channel-support for a helical-screw motion
    • A. Broomand, and F. Elinder Large-scale movement within the voltage-sensor paddle of a potassium channel-support for a helical-screw motion Neuron 59 2008 770 777
    • (2008) Neuron , vol.59 , pp. 770-777
    • Broomand, A.1    Elinder, F.2
  • 6
    • 34547569922 scopus 로고    scopus 로고
    • Mapping the electrostatic potential within the ribosomal exit tunnel
    • J. Lu, W.R. Kobertz, and C. Deutsch Mapping the electrostatic potential within the ribosomal exit tunnel J Mol Biol 371 2007 1378 1391
    • (2007) J Mol Biol , vol.371 , pp. 1378-1391
    • Lu, J.1    Kobertz, W.R.2    Deutsch, C.3
  • 7
    • 20444430500 scopus 로고    scopus 로고
    • Secondary structure formation of a transmembrane segment in Kv channels
    • J. Lu, and C. Deutsch Secondary structure formation of a transmembrane segment in Kv channels Biochemistry 44 2005 8230 8243
    • (2005) Biochemistry , vol.44 , pp. 8230-8243
    • Lu, J.1    Deutsch, C.2
  • 9
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • C.A. Woolhead, P.J. McCormick, and A.E. Johnson Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins Cell 116 2004 725 736
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 10
    • 77949270274 scopus 로고    scopus 로고
    • Alpha-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel
    • S. Bhushan, M. Gartmann, M. Halic, J.P. Armache, A. Jarasch, and T. Mielke et al. alpha-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel Nat Struct Mol Biol 17 2010 313 317
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 313-317
    • Bhushan, S.1    Gartmann, M.2    Halic, M.3    Armache, J.P.4    Jarasch, A.5    Mielke, T.6
  • 12
    • 0012249596 scopus 로고    scopus 로고
    • Different conformations of nascent polypeptides during translocation across the ER membrane
    • [Computer File]
    • I. Mingarro, I. Nilsson, P. Whitley, and G. von Heijne Different conformations of nascent polypeptides during translocation across the ER membrane BMC Cell Biol 1 2000 3 [Computer File]
    • (2000) BMC Cell Biol , vol.1 , pp. 3
    • Mingarro, I.1    Nilsson, I.2    Whitley, P.3    Von Heijne, G.4
  • 13
    • 17044363522 scopus 로고    scopus 로고
    • A cradle for new proteins: Trigger factor at the ribosome
    • T. Maier, L. Ferbitz, E. Deuerling, and N. Ban A cradle for new proteins: trigger factor at the ribosome Curr Opin Struct Biol 15 2005 204 212
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 204-212
    • Maier, T.1    Ferbitz, L.2    Deuerling, E.3    Ban, N.4
  • 14
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • G. Kramer, D. Boehringer, N. Ban, and B. Bukau The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins Nat Struct Mol Biol 16 2009 589 597
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 15
    • 84867255441 scopus 로고    scopus 로고
    • Compaction of a prokaryotic signal-anchor transmembrane domain begins within the ribosome tunnel and is stabilized by SRP during targeting
    • P.J. Robinson, J.E. Findlay, and C.A. Woolhead Compaction of a prokaryotic signal-anchor transmembrane domain begins within the ribosome tunnel and is stabilized by SRP during targeting J Mol Biol 423 2012 600 612
    • (2012) J Mol Biol , vol.423 , pp. 600-612
    • Robinson, P.J.1    Findlay, J.E.2    Woolhead, C.A.3
  • 16
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • S. Pechmann, F. Willmund, and J. Frydman The ribosome as a hub for protein quality control Mol Cell 49 2013 411 421
    • (2013) Mol Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 17
    • 64049105717 scopus 로고    scopus 로고
    • Tertiary interactions within the ribosomal exit tunnel
    • A. Kosolapov, and C. Deutsch Tertiary interactions within the ribosomal exit tunnel Nat Struct Mol Biol 16 2009 405 411
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 405-411
    • Kosolapov, A.1    Deutsch, C.2
  • 18
    • 33746592161 scopus 로고    scopus 로고
    • Molecular simulations of cotranslational protein folding: Fragment stabilities, folding cooperativity, and trapping in the ribosome
    • A.H. Elcock Molecular simulations of cotranslational protein folding: fragment stabilities, folding cooperativity, and trapping in the ribosome PLoS Comput Biol 2 2006 e98
    • (2006) PLoS Comput Biol , vol.2 , pp. 98
    • Elcock, A.H.1
  • 20
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum
    • M. Kowarik, S. Kung, B. Martoglio, and A. Helenius Protein folding during cotranslational translocation in the endoplasmic reticulum Mol Cell 10 2002 769 778
    • (2002) Mol Cell , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 21
    • 84862972129 scopus 로고    scopus 로고
    • Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate
    • D.A. Kelkar, A. Khushoo, Z. Yang, and W.R. Skach Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate J Biol Chem 287 2012 2568 2578
    • (2012) J Biol Chem , vol.287 , pp. 2568-2578
    • Kelkar, D.A.1    Khushoo, A.2    Yang, Z.3    Skach, W.R.4
  • 23
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • S.B. Long, E.B. Campbell, and R. MacKinnon Voltage sensor of Kv1.2: structural basis of electromechanical coupling Science 309 2005 903 908
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 24
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Y. Murata, H. Iwasaki, M. Sasaki, K. Inaba, and Y. Okamura Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor Nature 435 2005 1239 1243
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 25
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • M. Sasaki, M. Takagi, and Y. Okamura A voltage sensor-domain protein is a voltage-gated proton channel Science 312 2006 589 592
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 26
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • A.A. Alabi, M.I. Bahamonde, H.J. Jung, J.I. Kim, and K.J. Swartz Portability of paddle motif function and pharmacology in voltage sensors Nature 450 2007 370 375
    • (2007) Nature , vol.450 , pp. 370-375
    • Alabi, A.A.1    Bahamonde, M.I.2    Jung, H.J.3    Kim, J.I.4    Swartz, K.J.5
  • 27
    • 77955626630 scopus 로고    scopus 로고
    • + channel with a miniature engineered voltage sensor
    • + channel with a miniature engineered voltage sensor Cell 142 2010 580 589
    • (2010) Cell , vol.142 , pp. 580-589
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 28
    • 84869090494 scopus 로고    scopus 로고
    • Membrane protein TM segments are retained at the translocon during integration until the nascent chain cues FRET-detected release into bulk lipid
    • B. Hou, P.J. Lin, and A.E. Johnson Membrane protein TM segments are retained at the translocon during integration until the nascent chain cues FRET-detected release into bulk lipid Mol Cell 48 2012 398 408
    • (2012) Mol Cell , vol.48 , pp. 398-408
    • Hou, B.1    Lin, P.J.2    Johnson, A.E.3
  • 29
    • 69449085016 scopus 로고    scopus 로고
    • Dissecting the physiological role of selective transmembrane-segment retention at the ER translocon
    • B.C. Cross, and S. High Dissecting the physiological role of selective transmembrane-segment retention at the ER translocon J Cell Sci 122 2009 1768 1777
    • (2009) J Cell Sci , vol.122 , pp. 1768-1777
    • Cross, B.C.1    High, S.2
  • 30
    • 61949084073 scopus 로고    scopus 로고
    • Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum Sec61 translocon
    • D. Pitonzo, Z. Yang, Y. Matsumura, A.E. Johnson, and W.R. Skach Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum Sec61 translocon Mol Biol Cell 20 2009 685 698
    • (2009) Mol Biol Cell , vol.20 , pp. 685-698
    • Pitonzo, D.1    Yang, Z.2    Matsumura, Y.3    Johnson, A.E.4    Skach, W.R.5
  • 31
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actrions of two internal sequences
    • W. Skach, and V.R. Lingappa Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actrions of two internal sequences J Biol Chem 268 1993 23552 23561
    • (1993) J Biol Chem , vol.268 , pp. 23552-23561
    • Skach, W.1    Lingappa, V.R.2
  • 32
    • 0029738828 scopus 로고    scopus 로고
    • Biogenesis of polytopic membrane proteins: Membrane segments of P-glycoprotein sequentially translocate to span the ER membrane
    • A.C. Borel, and S.M. Simon Biogenesis of polytopic membrane proteins: membrane segments of P-glycoprotein sequentially translocate to span the ER membrane Biochemistry 35 1996 10587 10594
    • (1996) Biochemistry , vol.35 , pp. 10587-10594
    • Borel, A.C.1    Simon, S.M.2
  • 33
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein
    • H. Sadlish, D. Pitonzo, A.E. Johnson, and W.R. Skach Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein Nat Struct Mol Biol 12 2005 870 878
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 34
    • 38049058405 scopus 로고    scopus 로고
    • Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesis
    • Y. Kida, F. Morimoto, and M. Sakaguchi Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesis J Cell Biol 179 2007 1441 1452
    • (2007) J Cell Biol , vol.179 , pp. 1441-1452
    • Kida, Y.1    Morimoto, F.2    Sakaguchi, M.3
  • 35
    • 0035964418 scopus 로고    scopus 로고
    • Long-QT syndrome-associated missense mutations in the pore helix of the HERG
    • F.D. Huang, J. Chen, M. Lin, M.T. Keating, and M.C. Sanguinetti Long-QT syndrome-associated missense mutations in the pore helix of the HERG Circulation 104 2001 1071 1075
    • (2001) Circulation , vol.104 , pp. 1071-1075
    • Huang, F.D.1    Chen, J.2    Lin, M.3    Keating, M.T.4    Sanguinetti, M.C.5
  • 36
    • 33644851751 scopus 로고    scopus 로고
    • Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism
    • C.L. Anderson, B.P. Delisle, B.D. Anson, J.A. Kilby, M.L. Will, and D.J. Tester et al. Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism Circulation 113 2006 365 373
    • (2006) Circulation , vol.113 , pp. 365-373
    • Anderson, C.L.1    Delisle, B.P.2    Anson, B.D.3    Kilby, J.A.4    Will, M.L.5    Tester, D.J.6
  • 37
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289 2000 905 920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 38
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • P. Nissen, J. Hansen, N. Ban, P.B. Moore, and T.A. Steitz The structural basis of ribosome activity in peptide bond synthesis Science 289 2000 920 930
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 39
    • 0009576440 scopus 로고
    • Conformational properties of polypeptide chains
    • W. H. Freeman and Company New York, NY
    • T.E. Creighton Conformational properties of polypeptide chains Proteins 1993 W. H. Freeman and Company New York, NY 171 199
    • (1993) Proteins , pp. 171-199
    • Creighton, T.E.1
  • 41
    • 5144234840 scopus 로고    scopus 로고
    • Structure acquisition of the T1 domain of Kv1.3 during biogenesis
    • A. Kosolapov, L. Tu, J. Wang, and C. Deutsch Structure acquisition of the T1 domain of Kv1.3 during biogenesis Neuron 44 2004 295 307
    • (2004) Neuron , vol.44 , pp. 295-307
    • Kosolapov, A.1    Tu, L.2    Wang, J.3    Deutsch, C.4
  • 43
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • F. Bezanilla The voltage sensor in voltage-dependent ion channels Physiol Rev 80 2000 555 592
    • (2000) Physiol Rev , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 44
    • 20044389842 scopus 로고    scopus 로고
    • Membrane insertion of a potassium-channel voltage sensor
    • T. Hessa, S.H. White, and G. von Heijne Membrane insertion of a potassium-channel voltage sensor Science 307 2005 1427
    • (2005) Science , vol.307 , pp. 1427
    • Hessa, T.1    White, S.H.2    Von Heijne, G.3
  • 45
    • 0037039368 scopus 로고    scopus 로고
    • + channel, KAT1, into the endoplasmic reticulum membrane: Synergistic insertion of voltage-sensing segments, S3-S4, and independent insertion of pore-forming segments, S5-P-S6
    • + channel, KAT1, into the endoplasmic reticulum membrane: synergistic insertion of voltage-sensing segments, S3-S4, and independent insertion of pore-forming segments, S5-P-S6 Proc Natl Acad Sci USA 99 2002 60 65
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 60-65
    • Sato, Y.1    Sakaguchi, M.2    Goshima, S.3    Nakamura, T.4    Uozumi, N.5
  • 48
    • 84860390173 scopus 로고    scopus 로고
    • Contributions of counter-charge in a potassium channel voltage-sensor domain
    • S.A. Pless, J.D. Galpin, A.P. Niciforovic, and C.A. Ahern Contributions of counter-charge in a potassium channel voltage-sensor domain Nat Chem Biol 7 2011 617 623
    • (2011) Nat Chem Biol , vol.7 , pp. 617-623
    • Pless, S.A.1    Galpin, J.D.2    Niciforovic, A.P.3    Ahern, C.A.4
  • 50
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • B.D. Hamman, J.C. Chen, E.E. Johnson, and A.E. Johnson The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane Cell 89 1997 535 544
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.C.2    Johnson, E.E.3    Johnson, A.E.4
  • 51
    • 78049253482 scopus 로고    scopus 로고
    • Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
    • P.F. Egea, and R.M. Stroud Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes Proc Natl Acad Sci USA 107 2010 17182 17187
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17182-17187
    • Egea, P.F.1    Stroud, R.M.2
  • 53
    • 0002207938 scopus 로고
    • A fast algorithm for nonlinearity constrained optimization calculations
    • G.A. Watson, Springer-Verlag Berlin, Germany
    • M.J.D. Powell A fast algorithm for nonlinearity constrained optimization calculations G.A. Watson, Numerical Analysis 1978 Springer-Verlag Berlin, Germany
    • (1978) Numerical Analysis
    • Powell, M.J.D.1


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