-
1
-
-
0034610788
-
Three-dimensional structure of the ion-coupled transport protein NhaA
-
Analysis of two-dimensional crystals of NhaA by electron cryo-microcopy lead to a 7 Å resolution map of the protein in the plane of the membrane and a 14 Å resolution map vertical to the membrane. The three-dimensional map of the transporter revealed 12 tilted helices spanning the membrane. This structural map provides the first clues to the architecture of a transporter.
-
Williams K.A. Three-dimensional structure of the ion-coupled transport protein NhaA. Nature. 403:2000;112-115. Analysis of two-dimensional crystals of NhaA by electron cryo-microcopy lead to a 7 Å resolution map of the protein in the plane of the membrane and a 14 Å resolution map vertical to the membrane. The three-dimensional map of the transporter revealed 12 tilted helices spanning the membrane. This structural map provides the first clues to the architecture of a transporter.
-
(2000)
Nature
, vol.403
, pp. 112-115
-
-
Williams, K.A.1
-
2
-
-
0032478818
-
The structure of the potassium channel: Molecular basis of K+ conduction and selectivity
-
Doyle D.A., Cabral J.M., Pfuetzner R.A., Kuo A., Gulbis J.M., Cohen S.L., Chait B.T., MacKinnon R. The structure of the potassium channel: Molecular basis of K+ conduction and selectivity. Science. 280:1998;69-77.
-
(1998)
Science
, vol.280
, pp. 69-77
-
-
Doyle, D.A.1
Cabral, J.M.2
Pfuetzner, R.A.3
Kuo, A.4
Gulbis, J.M.5
Cohen, S.L.6
Chait, B.T.7
MacKinnon, R.8
-
3
-
-
0032545321
-
Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
-
Chang G., Spencer R.H., Lee A.T., Barclay M.T., Rees D.C. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:1998;2220-2225.
-
(1998)
Science
, vol.282
, pp. 2220-2225
-
-
Chang, G.1
Spencer, R.H.2
Lee, A.T.3
Barclay, M.T.4
Rees, D.C.5
-
4
-
-
0018987976
-
Intracellular protein topogenesis
-
Blobel G. Intracellular protein topogenesis. Proc Natl Acad Sci USA. 77:1980;1496-1500.
-
(1980)
Proc Natl Acad Sci USA
, vol.77
, pp. 1496-1500
-
-
Blobel, G.1
-
5
-
-
0019464222
-
The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
-
Engelman D.M., Steitz T.A. The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis. Cell. 23:1981;411-422.
-
(1981)
Cell
, vol.23
, pp. 411-422
-
-
Engelman, D.M.1
Steitz, T.A.2
-
6
-
-
0028170807
-
Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
-
Walter P., Johnson A.E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol. 10:1994;87-119.
-
(1994)
Annu Rev Cell Biol
, vol.10
, pp. 87-119
-
-
Walter, P.1
Johnson, A.E.2
-
7
-
-
0025854858
-
A Protein-conducting channel in the endoplasmic reticulum
-
Simon S.M., Blobel G. A Protein-conducting channel in the endoplasmic reticulum. Cell. 65:1991;371-380.
-
(1991)
Cell
, vol.65
, pp. 371-380
-
-
Simon, S.M.1
Blobel, G.2
-
8
-
-
0027985063
-
Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
-
Crowley K.S., Liao S., Worrell V.E., Reinhart G.D., Johnson A.E. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell. 78:1994;461-471.
-
(1994)
Cell
, vol.78
, pp. 461-471
-
-
Crowley, K.S.1
Liao, S.2
Worrell, V.E.3
Reinhart, G.D.4
Johnson, A.E.5
-
9
-
-
0345444027
-
Oligomeric rings of the Sec61 complex induced by ligands required for protein translocation
-
Hanein D., Matlack K.E., Jungnickel B., Plath K., Kalies K.U., Miller K.R., Rapoport T.A., Akey C.W. Oligomeric rings of the Sec61 complex induced by ligands required for protein translocation. Cell. 87:1996;721-732.
-
(1996)
Cell
, vol.87
, pp. 721-732
-
-
Hanein, D.1
Matlack, K.E.2
Jungnickel, B.3
Plath, K.4
Kalies, K.U.5
Miller, K.R.6
Rapoport, T.A.7
Akey, C.W.8
-
10
-
-
0030611388
-
The aqueous pore through the translocon has a diameter of 40 to 60 Å during cotranslational protein translocation at the ER membrane
-
Hamman B.D., Chen J.C., Johnson E.E., Johnson A.E. The aqueous pore through the translocon has a diameter of 40 to 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
-
11
-
-
0027424601
-
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
-
Gorlich D., Rapoport T.A. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell. 75:1993;615-630.
-
(1993)
Cell
, vol.75
, pp. 615-630
-
-
Gorlich, D.1
Rapoport, T.A.2
-
12
-
-
0028929094
-
The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum
-
Oliver J., Jungnickel B., Gorlich D., Rapoport T., High S. The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Lett. 362:1995;126-130.
-
(1995)
FEBS Lett
, vol.362
, pp. 126-130
-
-
Oliver, J.1
Jungnickel, B.2
Gorlich, D.3
Rapoport, T.4
High, S.5
-
13
-
-
0026504192
-
A protein of the endoplasmic reticulum involved early in polypeptide translocation
-
Gorlich D., Hartmann E., Prehn S., Rapoport T.A. A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature. 357:1993;47-52.
-
(1993)
Nature
, vol.357
, pp. 47-52
-
-
Gorlich, D.1
Hartmann, E.2
Prehn, S.3
Rapoport, T.A.4
-
14
-
-
0342995731
-
The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
-
Do H., Falcone D., Lin J., Andrews D.W., Johnson A.E. The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell. 85:1996;369-378.
-
(1996)
Cell
, vol.85
, pp. 369-378
-
-
Do, H.1
Falcone, D.2
Lin, J.3
Andrews, D.W.4
Johnson, A.E.5
-
15
-
-
0026794697
-
The E. coli ffh gene is necessary for viability and efficient protein export
-
Phillips G.J., Silhavy T.J. The E. coli ffh gene is necessary for viability and efficient protein export. Nature. 359:1992;744-746.
-
(1992)
Nature
, vol.359
, pp. 744-746
-
-
Phillips, G.J.1
Silhavy, T.J.2
-
16
-
-
0028338954
-
An alternative protein targeting pathway in Escherichia coli: Studies on the role of FtsY
-
Luirink J., ten Hagen-Jongman C.M., van der Weijden C.C., Oudega B., High S., Dobberstein B., Kusters R. An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY. EMBO J. 13:1994;2289-2296.
-
(1994)
EMBO J
, vol.13
, pp. 2289-2296
-
-
Luirink, J.1
Ten Hagen-Jongman, C.M.2
Van Der Weijden, C.C.3
Oudega, B.4
High, S.5
Dobberstein, B.6
Kusters, R.7
-
17
-
-
0027958547
-
Evolutionary conservation of components of the protein translocation complex
-
Hartmann E., Sommer T., Prehn S., Gorlich D., Jentsch S., Rapoport T.A. Evolutionary conservation of components of the protein translocation complex. Nature. 367:1994;654-657.
-
(1994)
Nature
, vol.367
, pp. 654-657
-
-
Hartmann, E.1
Sommer, T.2
Prehn, S.3
Gorlich, D.4
Jentsch, S.5
Rapoport, T.A.6
-
18
-
-
0031472242
-
The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
-
Ulbrandt N.D., Newitt J.A., Bernstein H.D. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell. 88:1997;187-196.
-
(1997)
Cell
, vol.88
, pp. 187-196
-
-
Ulbrandt, N.D.1
Newitt, J.A.2
Bernstein, H.D.3
-
19
-
-
0031020515
-
FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins
-
Seluanov A., Bibi E. FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins. J Biol Chem. 272:1997;2053-2055.
-
(1997)
J Biol Chem
, vol.272
, pp. 2053-2055
-
-
Seluanov, A.1
Bibi, E.2
-
20
-
-
0032816265
-
In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli
-
A cell-free system deficient in either Ffh, 4.5S RNA and FtsY or SecA/SecB was prepared. The membrane insertion of mannitol permease was dependent on both the addition of Ffh and FtsY. The export of pro-OmpA into urea-treated inverted membrane vesicles was blocked using these SecA/SecB/Ffh/FtsY-depleted extracts. Pro-OmpA export was restored by the addition of SecA and SecB, but not Ffh and FtsY. These results show that Ffh/FtsY specializes in the targeting of inner membrane proteins.
-
Koch H-G., Hengelage T., Neumann-Haefelin C., MacFarlane J., Hoffschulte H.K., Schimz K-L., Mechler B., Muller M. In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli. Mol Biol Cell. 10:1999;2163-2173. A cell-free system deficient in either Ffh, 4.5S RNA and FtsY or SecA/SecB was prepared. The membrane insertion of mannitol permease was dependent on both the addition of Ffh and FtsY. The export of pro-OmpA into urea-treated inverted membrane vesicles was blocked using these SecA/SecB/Ffh/FtsY-depleted extracts. Pro-OmpA export was restored by the addition of SecA and SecB, but not Ffh and FtsY. These results show that Ffh/FtsY specializes in the targeting of inner membrane proteins.
-
(1999)
Mol Biol Cell
, vol.10
, pp. 2163-2173
-
-
Koch, H.-G.1
Hengelage, T.2
Neumann-Haefelin, C.3
MacFarlane, J.4
Hoffschulte, H.K.5
Schimz, K.-L.6
Mechler, B.7
Muller, M.8
-
21
-
-
0034602846
-
Discrimination between SRP- And SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
-
Chemical crosslinking and site-specific photocrosslinking studies were used to show that Ffh recognizes the first signal anchor of mannitol permease. Mannitol permease is crosslinked specifically to Ffh. Trigger factor was shown to interact with nascent pro-OmpA, preventing binding of Ffh to pro-OmpA. Crosslinking studies show that trigger factor does not interact with ribosome bound-mannitol permease.
-
Beck K., Wu L-F., Brunner J., Muller M. Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J. 19:2000;134-143. Chemical crosslinking and site-specific photocrosslinking studies were used to show that Ffh recognizes the first signal anchor of mannitol permease. Mannitol permease is crosslinked specifically to Ffh. Trigger factor was shown to interact with nascent pro-OmpA, preventing binding of Ffh to pro-OmpA. Crosslinking studies show that trigger factor does not interact with ribosome bound-mannitol permease.
-
(2000)
EMBO J
, vol.19
, pp. 134-143
-
-
Beck, K.1
Wu, L.-F.2
Brunner, J.3
Muller, M.4
-
22
-
-
0030590843
-
Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle
-
de Gier J.W., Mansournia P., Valent Q.A., Phillips G.J., Luirink J., von Heijne G. Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle. FEBS Lett. 399:1996;307-309.
-
(1996)
FEBS Lett
, vol.399
, pp. 307-309
-
-
De Gier, J.W.1
Mansournia, P.2
Valent, Q.A.3
Phillips, G.J.4
Luirink, J.5
Von Heijne, G.6
-
23
-
-
0030959069
-
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
-
Duong F., Wickner W. Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. EMBO J. 16:1997;2756-2768.
-
(1997)
EMBO J
, vol.16
, pp. 2756-2768
-
-
Duong, F.1
Wickner, W.2
-
24
-
-
0345196631
-
The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
-
The SecY/E complex was purified from B. subtilis and reconstituted in proteoliposomes. These proteoliposomes were found to be translocation competent. Electron microscopy was performed on SecY/E complexes in detergent and proteoliposomes. The SecY/E complexes formed oligomeric ring structures similar to those formed by the eukaryotic Sec61p complex. The SecY/E rings are proposed to represent the protein-conducting channels of the bacterial inner membrane.
-
Meyer T.H., Menetret J-F., Breitling R., Miller K.R., Akey C.W., Rapoport T.A. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J Mol Biol. 285:1999;1789-1800. The SecY/E complex was purified from B. subtilis and reconstituted in proteoliposomes. These proteoliposomes were found to be translocation competent. Electron microscopy was performed on SecY/E complexes in detergent and proteoliposomes. The SecY/E complexes formed oligomeric ring structures similar to those formed by the eukaryotic Sec61p complex. The SecY/E rings are proposed to represent the protein-conducting channels of the bacterial inner membrane.
-
(1999)
J Mol Biol
, vol.285
, pp. 1789-1800
-
-
Meyer, T.H.1
Menetret, J.-F.2
Breitling, R.3
Miller, K.R.4
Akey, C.W.5
Rapoport, T.A.6
-
25
-
-
0034161573
-
SecYEG assembles into a tetramer to form the active protein translocation channel
-
Electron microscopy data show that solubilized B. subtilis SecYEG exists as either a monomer or dimer. The formation of membrane-inserted SecA, by the addition of SecA in the presence of AMP-PNP, triggers the formation of the SecYEG tetramer. The active translocase probably consists of a SecA homodimer and four SecYEG complexes, as revealed by the mass of the SecYEG active complex and by quantitation of SecA and SecY in the soluble translocase-precursor complex.
-
Manting E.H., van der Does C., Remigy H., Engel A., Driessen A.J.M. SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19:2000;852-861. Electron microscopy data show that solubilized B. subtilis SecYEG exists as either a monomer or dimer. The formation of membrane-inserted SecA, by the addition of SecA in the presence of AMP-PNP, triggers the formation of the SecYEG tetramer. The active translocase probably consists of a SecA homodimer and four SecYEG complexes, as revealed by the mass of the SecYEG active complex and by quantitation of SecA and SecY in the soluble translocase-precursor complex.
-
(2000)
EMBO J
, vol.19
, pp. 852-861
-
-
Manting, E.H.1
Van Der Does, C.2
Remigy, H.3
Engel, A.4
Driessen, A.J.M.5
-
26
-
-
0026464916
-
Membrane insertion of the mannitol permease of Escherichia coli occurs under conditions of impaired SecA functions
-
Werner P.K., Saier M.H. Jr., Muller M. Membrane insertion of the mannitol permease of Escherichia coli occurs under conditions of impaired SecA functions. J Biol Chem. 267:1992;24 523-24 532.
-
(1992)
J Biol Chem
, vol.267
, pp. 24523-24532
-
-
Werner, P.K.1
Saier, M.h.jr.2
Muller, M.3
-
27
-
-
85047694884
-
Alterations in the extracellular domain of M13 procoat protein make its membrane insertion dependent on secA and secY
-
Kuhn A. Alterations in the extracellular domain of M13 procoat protein make its membrane insertion dependent on secA and secY. Eur J Biochem. 177:1988;261-271.
-
(1988)
Eur J Biochem
, vol.177
, pp. 261-271
-
-
Kuhn, A.1
-
28
-
-
0027473683
-
Sec dependent and sec independent assembly of E. coli inner membrane proteins: The topological rules depend on chain length
-
Andersson H., von Heijne G. Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length. EMBO J. 12:1993;683-691.
-
(1993)
EMBO J
, vol.12
, pp. 683-691
-
-
Andersson, H.1
Von Heijne, G.2
-
29
-
-
0029831038
-
Chaperonin-promoted post-translational membrane insertion of a multispanning membrane protein lactose permease
-
Bochkareva E., Seluanov A., Bibi E., Girshovich A. Chaperonin-promoted post-translational membrane insertion of a multispanning membrane protein lactose permease. J Biol Chem. 271:1996;22 256-22 261.
-
(1996)
J Biol Chem
, vol.271
, pp. 22256-22261
-
-
Bochkareva, E.1
Seluanov, A.2
Bibi, E.3
Girshovich, A.4
-
30
-
-
0031983038
-
Co- And posttranslational translocation mechanism direct cystic fibrosis transmembrane conducting conductance regulator N terminus transmembrane assembly
-
Lu Y., Xiong X., Helm A., Kimani K., Bragin A., Skach W.R. Co- and posttranslational translocation mechanism direct cystic fibrosis transmembrane conducting conductance regulator N terminus transmembrane assembly. J Biol Chem. 273:1998;568-576.
-
(1998)
J Biol Chem
, vol.273
, pp. 568-576
-
-
Lu, Y.1
Xiong, X.2
Helm, A.3
Kimani, K.4
Bragin, A.5
Skach, W.R.6
-
31
-
-
0034142228
-
Transmembrane biogenesis of Kv1.3
-
The insertion of the Shaker-like Kv channel into the endoplasmic reticulum membrane was studied using an in vitro translation and translocation system. The data showed that transmembrane segments 1, 2, 3, 5 and 6 can initiate translocation, but with varying degrees of efficiency. Carbonate-extraction assays showed that transmembrane segments 3 and 6 fail to integrate into the membrane. Examining insertion of multiple transmembrane segments revealed that the hydrophobic regions cooperate during membrane insertion. Surprisingly, the first transmembrane segments does not initiate carboxy-terminal translocation. Rather, the second transmembrane segment does, which was expected to have no role in initiating translocation.
-
Tu L., Wang J., Helm A., Skach W.R., Deutsch C. Transmembrane biogenesis of Kv1.3. Biochem. 39:2000;824-836. The insertion of the Shaker-like Kv channel into the endoplasmic reticulum membrane was studied using an in vitro translation and translocation system. The data showed that transmembrane segments 1, 2, 3, 5 and 6 can initiate translocation, but with varying degrees of efficiency. Carbonate-extraction assays showed that transmembrane segments 3 and 6 fail to integrate into the membrane. Examining insertion of multiple transmembrane segments revealed that the hydrophobic regions cooperate during membrane insertion. Surprisingly, the first transmembrane segments does not initiate carboxy-terminal translocation. Rather, the second transmembrane segment does, which was expected to have no role in initiating translocation.
-
(2000)
Biochem
, vol.39
, pp. 824-836
-
-
Tu, L.1
Wang, J.2
Helm, A.3
Skach, W.R.4
Deutsch, C.5
-
32
-
-
0025675488
-
The function of a leader peptide in translocating charged amino acyl residues across a membrane
-
Rohrer J., Kuhn A. The function of a leader peptide in translocating charged amino acyl residues across a membrane. Science. 250:1990;1418-1421.
-
(1990)
Science
, vol.250
, pp. 1418-1421
-
-
Rohrer, J.1
Kuhn, A.2
-
33
-
-
0027284115
-
Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule
-
Zhang J.T., Duthie M., Ling V. Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule. J Biol Chem. 268:1993;15 101-15 110.
-
(1993)
J Biol Chem
, vol.268
, pp. 15101-15110
-
-
Zhang, J.T.1
Duthie, M.2
Ling, V.3
-
34
-
-
0031946150
-
Dissection of de novo membrane insertion activities of internal transmembrane segments of ATP-binding-cassette transporters: Toward understanding topological rules for membrane assembly of polytopic membrane proteins
-
Zhang J-T., Chen M., Han E., Wang C. Dissection of de novo membrane insertion activities of internal transmembrane segments of ATP-binding-cassette transporters: toward understanding topological rules for membrane assembly of polytopic membrane proteins. Mol Biol Cell. 9:1998;853-863.
-
(1998)
Mol Biol Cell
, vol.9
, pp. 853-863
-
-
Zhang, J.-T.1
Chen, M.2
Han, E.3
Wang, C.4
-
35
-
-
0028175016
-
Topological "frustration" in multispanning E. coli inner membrane proteins
-
Gafvelin G., von Heijne G. Topological "frustration" in multispanning E. coli inner membrane proteins. Cell. 77:1994;401-412.
-
(1994)
Cell
, vol.77
, pp. 401-412
-
-
Gafvelin, G.1
Von Heijne, G.2
-
36
-
-
0029852326
-
Efficient insertion of odd-numbered transmembrane segments of the tetracycline resistance protein requires even-numbered segments
-
Guo D., Liu J., Motlagh A., Jewell J., Miller K.W. Efficient insertion of odd-numbered transmembrane segments of the tetracycline resistance protein requires even-numbered segments. J Biol Chem. 271:1996;30 829-30 834.
-
(1996)
J Biol Chem
, vol.271
, pp. 30829-30834
-
-
Guo, D.1
Liu, J.2
Motlagh, A.3
Jewell, J.4
Miller, K.W.5
-
37
-
-
0032561457
-
Assessment of topogenic functions of anticipated transmembrane segments of human band 3
-
Ota K., Sakaguchi M., Hamasaki N., Mihara K. Assessment of topogenic functions of anticipated transmembrane segments of human band 3. J Biol Chem. 273:1998;28 286-28 291.
-
(1998)
J Biol Chem
, vol.273
, pp. 28286-28291
-
-
Ota, K.1
Sakaguchi, M.2
Hamasaki, N.3
Mihara, K.4
-
38
-
-
0026581658
-
Membrane protein spanning segments as export signals
-
Calamia J., Manoil C. Membrane protein spanning segments as export signals. J Mol Biol. 224:1992;539-543.
-
(1992)
J Mol Biol
, vol.224
, pp. 539-543
-
-
Calamia, J.1
Manoil, C.2
-
39
-
-
0029817931
-
Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
-
Wilkinson B.M., Critchley A.J., Stirling C.J. Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J Biol Chem. 271:1996;25 590-25 597.
-
(1996)
J Biol Chem
, vol.271
, pp. 25590-25597
-
-
Wilkinson, B.M.1
Critchley, A.J.2
Stirling, C.J.3
-
40
-
-
0034053280
-
Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane
-
This study shows that translocation of the amino-terminal tail of ProW into the endoplasmic reticulum membrane is inefficient when less then four transmembrane segments are present. Most of these ProW constructs adopt an inverted membrane topology, as shown by a glycosylation assay. The results reveal that distant downstream determinants can control the insertion of the amino tail of a multispanning membrane protein into the ER membrane.
-
Nilsson I., Witt S., Kiefer H., Mingarro I., von Heijne G. Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane. J Biol Chem. 275:2000;6207-6213. This study shows that translocation of the amino-terminal tail of ProW into the endoplasmic reticulum membrane is inefficient when less then four transmembrane segments are present. Most of these ProW constructs adopt an inverted membrane topology, as shown by a glycosylation assay. The results reveal that distant downstream determinants can control the insertion of the amino tail of a multispanning membrane protein into the ER membrane.
-
(2000)
J Biol Chem
, vol.275
, pp. 6207-6213
-
-
Nilsson, I.1
Witt, S.2
Kiefer, H.3
Mingarro, I.4
Von Heijne, G.5
-
41
-
-
0032566739
-
Test the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein
-
Sato M., Hresko R., Mueckler M. Test the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein. J Biol Chem. 273:1998;25 203-25 208.
-
(1998)
J Biol Chem
, vol.273
, pp. 25203-25208
-
-
Sato, M.1
Hresko, R.2
Mueckler, M.3
-
42
-
-
0342351613
-
Predicting the orientation of eukaryotic membrane-spanning proteins
-
Hartmann E., Rapoport T.A., Lodish H.F. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc Natl Acad Sci USA. 86:1989;5786-5790.
-
(1989)
Proc Natl Acad Sci USA
, vol.86
, pp. 5786-5790
-
-
Hartmann, E.1
Rapoport, T.A.2
Lodish, H.F.3
-
43
-
-
0023782388
-
Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
-
Wessel H.P., Spiess M. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell. 55:1988;61-70.
-
(1988)
Cell
, vol.55
, pp. 61-70
-
-
Wessel, H.P.1
Spiess, M.2
-
44
-
-
0028304680
-
Membrane proteins: From sequence to structure
-
von Heijne G. Membrane proteins: from sequence to structure. Annu Rev Biophys Biomol Struct. 23:1994;167-192.
-
(1994)
Annu Rev Biophys Biomol Struct
, vol.23
, pp. 167-192
-
-
Von Heijne, G.1
-
45
-
-
0025947624
-
Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal
-
Ehrmann M., Beckwith J. Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal. J Biol Chem. 266:1991;16 530-16 533.
-
(1991)
J Biol Chem
, vol.266
, pp. 16530-16533
-
-
Ehrmann, M.1
Beckwith, J.2
-
46
-
-
0029894267
-
Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration
-
Borel A.C., Simon S.M. Biogenesis of polytopic membrane proteins: membrane segments assemble within translocation channels prior to membrane integration. Cell. 85:1996;379-389.
-
(1996)
Cell
, vol.85
, pp. 379-389
-
-
Borel, A.C.1
Simon, S.M.2
-
47
-
-
0030825974
-
Molecular mechanism of membrane protein integration into the endoplasmic reticulum
-
Mothes W., Heinrich S.U., Graf R., Nilsson I., von Heijne G., Brunner J., Rapoport T.A. Molecular mechanism of membrane protein integration into the endoplasmic reticulum. Cell. 89:1997;523-533.
-
(1997)
Cell
, vol.89
, pp. 523-533
-
-
Mothes, W.1
Heinrich, S.U.2
Graf, R.3
Nilsson, I.4
Von Heijne, G.5
Brunner, J.6
Rapoport, T.A.7
-
48
-
-
0029002962
-
The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
-
Martoglio B., Hofmann M.W., Brunner J., Dobberstein B. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell. 81:1995;207-214.
-
(1995)
Cell
, vol.81
, pp. 207-214
-
-
Martoglio, B.1
Hofmann, M.W.2
Brunner, J.3
Dobberstein, B.4
-
49
-
-
0031471055
-
Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
-
Liao S., Lin J., Do H., Johnson A.E. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell. 90:1997;31-41.
-
(1997)
Cell
, vol.90
, pp. 31-41
-
-
Liao, S.1
Lin, J.2
Do, H.3
Johnson, A.E.4
-
50
-
-
0030805752
-
Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor
-
Valent Q.A., de Gier J-W.L., von Heijne G., Kendall D.A., ten Hagen-Jongman C.M., Oudega B., Luirink J. Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor. Mol Microbiol. 25:1997;53-64.
-
(1997)
Mol Microbiol
, vol.25
, pp. 53-64
-
-
Valent, Q.A.1
De Gier, J.-W.L.2
Von Heijne, G.3
Kendall, D.A.4
Ten Hagen-Jongman, C.M.5
Oudega, B.6
Luirink, J.7
-
51
-
-
0034651753
-
YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
-
Photocrosslinking data is presented showing that the hydrophobic membrane anchor of inner membrane protein FtsQ comes into contact with lipids and YidC. Very little crosslinking takes place when the photoprobe is introduced in the hydrophilic regions that flank the hydrophobic region. Purification of the SecYEG translocase using a His tag at the amino terminus of SecY reveals that YidC is associated with the complex.
-
Scotti P.A., Urbanus M.L., Brunner J., de Gier J-W.L., von Heijne G., van der Does C.J.M., Driessen A.J.M., Oudega B., Luirink J. YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. EMBO J. 19:2000;542-549. Photocrosslinking data is presented showing that the hydrophobic membrane anchor of inner membrane protein FtsQ comes into contact with lipids and YidC. Very little crosslinking takes place when the photoprobe is introduced in the hydrophilic regions that flank the hydrophobic region. Purification of the SecYEG translocase using a His tag at the amino terminus of SecY reveals that YidC is associated with the complex.
-
(2000)
EMBO J
, vol.19
, pp. 542-549
-
-
Scotti, P.A.1
Urbanus, M.L.2
Brunner, J.3
De Gier, J.-W.L.4
Von Heijne, G.5
Van Der Does, C.J.M.6
Driessen, A.J.M.7
Oudega, B.8
Luirink, J.9
-
52
-
-
0022001799
-
Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli
-
Wolfe P.B., Rice M., Wickner W. Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli. J Biol Chem. 260:1985;1836-1841.
-
(1985)
J Biol Chem
, vol.260
, pp. 1836-1841
-
-
Wolfe, P.B.1
Rice, M.2
Wickner, W.3
-
53
-
-
0032430831
-
Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli
-
de Gier J.W., Scotti P.A., Saaf A., Valent Q.A., Kuhn A., Luirink J., von Heijne G. Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli. Proc Natl Acad Sci USA. 95:1998;14 646-14 651.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 14646-14651
-
-
De Gier, J.W.1
Scotti, P.A.2
Saaf, A.3
Valent, Q.A.4
Kuhn, A.5
Luirink, J.6
Von Heijne, G.7
-
54
-
-
0032079702
-
The Escherichia coli SRP and SecB targeting pathways converge at the translocon
-
Valent Q.A., Scotti P.A., High S., de Gier J-W.L., von Heijne G., Lentzen G., Wintermeyer W., Oudega B., Luirink J. The Escherichia coli SRP and SecB targeting pathways converge at the translocon. EMBO J. 17:1998;2504-2512.
-
(1998)
EMBO J
, vol.17
, pp. 2504-2512
-
-
Valent, Q.A.1
Scotti, P.A.2
High, S.3
De Gier, J.-W.L.4
Von Heijne, G.5
Lentzen, G.6
Wintermeyer, W.7
Oudega, B.8
Luirink, J.9
-
55
-
-
0026516666
-
Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion
-
Lee J-I., Kuhn A., Dalbey R.E. Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion. J Biol Chem. 267:1992;938-943.
-
(1992)
J Biol Chem
, vol.267
, pp. 938-943
-
-
Lee, J.-I.1
Kuhn, A.2
Dalbey, R.E.3
-
56
-
-
0034632819
-
YidC mediates membrane protein insertion in bacteria
-
in press. This paper shows for the first time in bacteria that YidC, which has homologs in mitochondria and chloroplasts, is required for the membrane insertion of two Sec-independent proteins. YidC is also shown to be essential for cell viability. Depletion of YidC interferes with the insertion of Sec-dependent membrane proteins, while having a minor effect on the export of proteins to the periplasmic space or outer membrane. The results provide evidence of a new protein that participates in the membrane insertion process.
-
Samuelson J.C., Chen M., Jiang F., Moller I., Wiedmann M., Kuhn A., Phillips G.J., Dalbey R.E. YidC mediates membrane protein insertion in bacteria. Nature. 2000;. in press. This paper shows for the first time in bacteria that YidC, which has homologs in mitochondria and chloroplasts, is required for the membrane insertion of two Sec-independent proteins. YidC is also shown to be essential for cell viability. Depletion of YidC interferes with the insertion of Sec-dependent membrane proteins, while having a minor effect on the export of proteins to the periplasmic space or outer membrane. The results provide evidence of a new protein that participates in the membrane insertion process.
-
(2000)
Nature
-
-
Samuelson, J.C.1
Chen, M.2
Jiang, F.3
Moller, I.4
Wiedmann, M.5
Kuhn, A.6
Phillips, G.J.7
Dalbey, R.E.8
-
57
-
-
0030656514
-
Oxa1p mediates the export of the N- And C-termini of pCoxII from the mitochondrial matrix to the intermembrane space
-
Hell K., Herrmann J., Pratje E., Neupert W., Stuart R.A. Oxa1p mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space. FEBS Lett. 418:1997;367-370.
-
(1997)
FEBS Lett
, vol.418
, pp. 367-370
-
-
Hell, K.1
Herrmann, J.2
Pratje, E.3
Neupert, W.4
Stuart, R.A.5
-
58
-
-
0032478139
-
Oxa1p, an essential component of the N-tail protein export machinery in mitochondria
-
Hell K., Herrmann J.M., Pratje E., Neupert W., Stuart R.A. Oxa1p, an essential component of the N-tail protein export machinery in mitochondria. Proc Natl Acad Sci USA. 95:1998;2250-2255.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 2250-2255
-
-
Hell, K.1
Herrmann, J.M.2
Pratje, E.3
Neupert, W.4
Stuart, R.A.5
-
59
-
-
0034695557
-
Chloroplast Oxa1p homolog Albino3 required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
-
This paper provides data that the antibody against Albino3 blocks the integration of the light harvesting chlorophyll-binding protein (LHCP) into thylakoid membranes. Preimmune serum does not inhibit insertion of LHCP. The antibody against Albino3 does not inhibit the export of proteins that use the Sec pathway or the delta pH pathway. Therefore, the authors conclude that Albino3 is part of a novel translocation system.
-
Misty Moore M., Harrison S., Peterson E.C., Henry R. Chloroplast Oxa1p homolog Albino3 required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes. J Biol Chem. 275:2000;1529-1532. This paper provides data that the antibody against Albino3 blocks the integration of the light harvesting chlorophyll-binding protein (LHCP) into thylakoid membranes. Preimmune serum does not inhibit insertion of LHCP. The antibody against Albino3 does not inhibit the export of proteins that use the Sec pathway or the delta pH pathway. Therefore, the authors conclude that Albino3 is part of a novel translocation system.
-
(2000)
J Biol Chem
, vol.275
, pp. 1529-1532
-
-
Misty Moore, M.1
Harrison, S.2
Peterson, E.C.3
Henry, R.4
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