Delivering proteins for export from the cytosol

被引:163
作者
Cross, Benedict C. S. [1 ]
Sinning, Irmgard [2 ]
Luirink, Joen [3 ]
High, Stephen [1 ]
机构
[1] Univ Manchester, Fac Life Sci, Manchester M13 9PT, Lancs, England
[2] Heidelberg Univ, Zentrum Biochem, D-69120 Heidelberg, Germany
[3] Vrije Univ Amsterdam, Fac Earth & Life Sci, NL-1081 HV Amsterdam, Netherlands
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
SIGNAL-RECOGNITION PARTICLE; ENDOPLASMIC-RETICULUM MEMBRANE; F1F0 ATP SYNTHASE; BACTERIAL CYTOPLASMIC MEMBRANE; MESSENGER-RNA LOCALIZATION; TAIL-ANCHORED PROTEINS; COLI INNER MEMBRANE; ESCHERICHIA-COLI; CHAPERONE SECB; PRESECRETORY PROTEINS;
D O I
10.1038/nrm2657
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Correct protein function depends on delivery to the appropriate cellular or subcellular compartment. Following the initiation of protein synthesis in the cytosol, many bacterial and eukaryotic proteins must be integrated into or transported across a membrane to reach their site of function. Whereas in the post-translational delivery pathway ATP-dependent factors bind to completed polypeptides and chaperone them until membrane translocation is initiated, a GTP-dependent co-translational pathway operates to couple ongoing protein synthesis to membrane transport. These distinct pathways provide different solutions for the maintenance of proteins in a state that is competent for membrane translocation and their delivery for export from the cytosol.
引用
收藏
页码:255 / 264
页数:10
相关论文
共 113 条
[1]   Signal recognition particle mediates post-translational targeting in eukaryotes [J].
Abell, BM ;
Pool, MR ;
Schlenker, O ;
Sinning, I ;
High, S .
EMBO JOURNAL, 2004, 23 (14) :2755-2764
[2]   The presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal-recognition particle in Escherichia coli [J].
Adams, H ;
Scotti, PA ;
de Cock, H ;
Luirink, J ;
Tommassen, J .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (22) :5564-5571
[3]   FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon [J].
Angelini, S ;
Deitermann, S ;
Koch, HG .
EMBO REPORTS, 2005, 6 (05) :476-481
[4]   Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites [J].
Angelini, Sandra ;
Boy, Diana ;
Schiltz, Emile ;
Koch, Hans-Georg .
JOURNAL OF CELL BIOLOGY, 2006, 174 (05) :715-724
[5]   Defining the role of the Escherichia coli chaperone SecB using comparative proteomics [J].
Baars, L ;
Ytterberg, AJ ;
Drew, D ;
Wagner, S ;
Thilo, C ;
van Wijk, KJ ;
de Gier, JW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (15) :10024-10034
[6]   Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting [J].
Bacher, G ;
Lutcke, H ;
Jungnickel, B ;
Rapoport, TA ;
Dobberstein, B .
NATURE, 1996, 381 (6579) :248-251
[7]   Protein translocation: Checkpoint role for SRP GTPase activation [J].
Bange, Gert ;
Wild, Klemens ;
Sinning, Irmgard .
CURRENT BIOLOGY, 2007, 17 (22) :R980-R982
[8]   Improved prediction of signal peptides: SignalP 3.0 [J].
Bendtsen, JD ;
Nielsen, H ;
von Heijne, G ;
Brunak, S .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 340 (04) :783-795
[9]   How tails guide tail-anchored proteins to their destinations [J].
Borgese, Nica ;
Brambillasca, Silvia ;
Colombo, Sara .
CURRENT OPINION IN CELL BIOLOGY, 2007, 19 (04) :368-375
[10]   Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel [J].
Bornemann, Thomas ;
Joeckel, Johannes ;
Rodnina, Marina V. ;
Wintermeyer, Wolfgang .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2008, 15 (05) :494-499