Abstract
All living organisms possess the ability to translocate proteins across biological membranes. This is a fundamental necessity since proteins function in different locations yet are synthesized in one compartment only, the cytosol. Even though different transport systems exist, the pathway that is dominandy used to translocate secretory and membrane proteins is known as the cotranslational transport pathway. It evolved only once and is in its core conserved throughout all kingdoms of life. The process is characterized by a well understood sequence of events: first, an N-terminal signal sequence of a nascent polypeptide is recognized on the ribosome by the signal recognition particle (SRP), then the SRP-ribosome complex is targeted to the membrane via the SRP receptor. Next, the nascent chain is transferred from SRP to the protein conducting channel, through which it is cotranslationally threaded. All the essential components of the system have been identified. Recent structural and biochemical studies have unveiled some of the intricate regulatory circuitry of the process. These studies also shed light on the accessory components unique to eukaryotes, pointing to early events in eukaryotic evolution.
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References
von Heijne G. Signal sequences. The limits of variation. J Mol Biol 1985; 184:99–105.
Matlin KS. The strange case of the signal recognition particle. Nat Rev Mol Cell Biol 2002; 3:538–542.
Doudna JA, Batey RT. Structural insights into the signal recognition particle. Annu Rev Biochem 2004; 73:539–557.
Egea PF, Stroud RM, Walter P. Targeting proteins to membranes: Structure of the signal recognition particle. Curr Opin Struct Biol 2005; 15:213–220.
Halic M, Beckmann R. The signal recognition particle and its interactions during protein targeting. Curr Opin Struct Biol 2005; 15:116–125.
Keenan RJ, Freymann DM, Stroud RM et al. The signal recognition particle. Annu Rev Biochem 2001; 70:755–775.
Pool MR. Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review). Mol Membr Biol 2005; 22:3–15.
Walter P, Blobel G. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature 1982; 299:691–698.
Leipe DD, Wolf YI, Koonin EV et al. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 2002; 317:41–72.
Halic M, Becker T, Pool MR et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 2004; 427:808–814.
Van Nues RW, Brown JD. Saccharomyces SRP RNA secondary structures: A conserved S-domain and extended Alu-domain. RNA 2004; 10:75–89.
Zwieb C, Eichler J. Getting on target: The archaeal signal recognition particle. Archaea 2002; 1:27–34.
Powers T, Walter P. Cotranslational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. Embo J 1997; 16:4880–4886.
Gilmore R, Walter P, Blobel G. Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J Cell Biol 1982; 95:470–477.
de Leeuw E, Poland D, Mol O et al. Membrane association of FtsY, the E. coli SRP receptor. FEBS Lett 1997; 416:225–229.
Bibi E, Herskovits AA, Bochkareva ES et al. Putative integral membrane SRP receptors. Trends Biochem Sci 2001; 26:15–16.
Zelazny A, Seluanov A, Cooper A et al. The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide. Proc Natl Acad Sci USA 1997; 94:6025–6029.
Young JC, Ursini J, Legate KR et al. An amino-terminal domain containing hydrophobic and hydrophilic sequences binds the signal recognition particle receptor alpha subunit to the beta subunit on the endoplasmic reticulum membrane. J Biol Chem 1995; 270:15650–15657.
Schwartz T, Blobel G. Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor. Cell 2003; 112:793–803.
Simon SM, Blobel G. A protein-conducting channel in the endoplasmic reticulum. Cell 1991; 65:371–380.
Hartmann E, Sommer T, Prehn S et al. Evolutionary conservation of components of the protein translocation complex. Nature 1994; 367:654–657.
Van den Berg B, Clemons Jr WM, Collinson I et al. X-ray structure of a protein-conducting channel. Nature 2004; 427:36–44.
Beckmann R, Spahn CM, Eswar N et al. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 2001; 107:361–372.
Collinson I, Breyton C, Duong F et al. Projection structure and oligomeric properties of a bacterial core protein translocase. Embo J 2001; 20:2462–2471.
Menetret JF, Hegde RS, Heinrich SU et al. Architecture of the ribosome-channel complex derived from native membranes. J Mol Biol 2005; 348:445–457.
Morgan DG, Menetret JF, Neuhof A et al. Structure of the mammalian ribosome-channel complex at 17A resolution. J Mol Biol 2002; 324:871–886.
Vetter IR, Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 2001; 294:1299–1304.
Romisch K, Webb J, Lingelbach K et al. The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain. J Cell Biol 1990; 111:1793–1802.
Zopf D, Bernstein HD, Johnson AE et al. The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. Embo J 1990; 9:4511–4517.
Bacher G, Lutcke H, Jungnickel B et al. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 1996; 381:248–251.
Powers T, Walter P. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 1995; 269:1422–1424.
Egea PF, Shan SO, Napetschnig J et al. Substrate twinning activates the signal recognition particle and its receptor. Nature 2004; 427:215–221.
Focia PJ, Shepotinovskaya IV, Scidler JA et al. Heterodimeric GTPase core of the SRP targeting complex. Science 2004; 303:373–377.
Herskovits AA, Shimoni E, Minsky A et al. Accumulation of endoplasmic membranes and novel membrane-bound ribosome-signal recognition particle receptor complexes in Escherichia coli. J Cell Biol 2002; 159:403–410.
Legate KR, Andrews DW. The beta-subunit of the signal recognition particle receptor is a novel GTP-binding protein without intrinsic GTPase activity. J Biol Chem 2003; 278:27712–27720.
Song W, Raden D, Mandon EC et al. Role of Sec61 alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel. Cell 2000; 100:333–343.
Stephenson K. Sec-dependent protein translocation across biological membranes: Evolutionary conservation of an essential protein transport pathway (review). Mol Membr Biol 2005; 22:17–28.
Gorlich D, Rapoport TA. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 1993; 75:615–630.
Bolhuis A. The archaeal Sec-dependent protein translocation pathway. Philos Trans R Soc Lond B Biol Sci 2004; 359:919–927.
Nakamura K, Yahagi S, Yamazaki T et al. Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA. J Biol Chem 1999; 274:13569–13576.
Caetano-Anolles G, Caetano-Anolles D. Universal sharing patterns in proteomes and evolution of protein fold architecture and life. J Mol Evol 2005; 60:484–498.
Chothia C, Gough J, Vogel C et al. Evolution of the protein repertoire. Science 2003; 300:1701–1703.
Sprang SR. G protein mechanisms: Insights from structural analysis. Annu Rev Biochem 1997; 66:639–678.
Jekely G. Small GTPases and the evolution of the eukaryotic cell. Bioessays 2003; 25:1129–1138.
Nie Z, Hirsch DS, Randazzo PA. Arf and its many interactors. Curr Opin Cell Biol 2003; 15:396–404.
Pasqualato S, Renault L, Cherfils J. Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for ‘front-back’ communication. EMBO Rep 2002; 3:1035–1041.
Lee MC, Orci L, Hamamoto S et al. Sarlp N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 2005; 122:605–617.
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Schwartz, T.U. (2007). Origins and Evolution of Cotranslational Transport to the ER. In: Eukaryotic Membranes and Cytoskeleton. Advances in Experimental Medicine and Biology, vol 607. Springer, New York, NY. https://doi.org/10.1007/978-0-387-74021-8_4
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DOI: https://doi.org/10.1007/978-0-387-74021-8_4
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