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Journal articles on the topic 'Signal recognition particle (SRP)'

Author: Grafiati

Published: 7 June 2025

Last updated: 16 July 2025

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1

Connolly, T., and R. Gilmore. "GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor." Journal of Cell Biology 123, no. 4 (1993): 799–807. http://dx.doi.org/10.1083/jcb.123.4.799.

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Translocation of proteins across the endoplasmic reticulum membrane is a GTP-dependent process. The signal recognition particle (SRP) and the SRP receptor both contain subunits with GTP binding domains. One GTP-dependent reaction during protein translocation is the SRP receptor-mediated dissociation of SRP from the signal sequence of a nascent polypeptide. Here, we have assayed the SRP and the SRP receptor for GTP binding and hydrolysis activities. GTP hydrolysis by SRP was not detected, so the maximal GTP hydrolysis rate for SRP was estimated to be &lt; 0.002 mol GTP hydrolyzed x mol of S

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2

Leung, Eileen, and Jeremy D. Brown. "Biogenesis of the signal recognition particle." Biochemical Society Transactions 38, no. 4 (2010): 1093–98. http://dx.doi.org/10.1042/bst0381093.

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Assembly of ribonucleoprotein complexes is a facilitated quality-controlled process that typically includes modification to the RNA component from precursor to mature form. The SRP (signal recognition particle) is a cytosolic ribonucleoprotein that catalyses protein targeting to the endoplasmic reticulum. Assembly of SRP is largely nucleolar, and most of its protein components are required to generate a stable complex. A pre-SRP is exported from the nucleus to the cytoplasm where the final protein, Srp54p, is incorporated. Although this outline of the SRP assembly pathway has been determined,

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3

Robinson, A., O. M. R. Westwood, and B. M. Austen. "Interactions of signal peptides with signal-recognition particle." Biochemical Journal 266, no. 1 (1990): 149–56. http://dx.doi.org/10.1042/bj2660149.

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The mechanisms whereby isolated or synthetic signal peptides inhibit processing of newly synthesized prolactin in microsome-supplemented lysates from reticulocytes and wheat-germ were investigated. At a concentration of 5 microM, a consensus signal peptide reverses the elongation arrest imposed by the signal-recognition particle (SRP), and at higher concentrations in addition inhibits elongation of both secretory and non-secretory proteins. A photoreactive form of a synthetic signal peptide cross-links under u.v. illumination to the 54 kDa and 68 kDa subunits of SRP, whereas the major cross-li

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4

Zwieb, Christian, and Shakhawat Bhuiyan. "Archaea Signal Recognition Particle Shows the Way." Archaea 2010 (2010): 1–11. http://dx.doi.org/10.1155/2010/485051.

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Archaea SRP is composed of an SRP RNA molecule and two bound proteins named SRP19 and SRP54. Regulated by the binding and hydrolysis of guanosine triphosphates, the RNA-bound SRP54 protein transiently associates not only with the hydrophobic signal sequence as it emerges from the ribosomal exit tunnel, but also interacts with the membrane-associated SRP receptor (FtsY). Comparative analyses of the archaea genomes and their SRP component sequences, combined with structural and biochemical data, support a prominent role of the SRP RNA in the assembly and function of the archaea SRP. The 5e motif

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5

Bovia, F., and K. Strub. "The signal recognition particle and related small cytoplasmic ribonucleoprotein particles." Journal of Cell Science 109, no. 11 (1996): 2601–8. http://dx.doi.org/10.1242/jcs.109.11.2601.

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Recently, a number of novel small cytoplasmic ribonucleoprotein particles have been identified that comprise RNA and protein subunits related to the signal recognition particle (SRP). Here we discuss the latest results on the structure and functions of SRP together with the structures and putative functions of the novel SRP-related ribonucleoprotein particles.

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6

Zwieb, C., and N. Larsen. "The signal recognition particle (SRP) database." Nucleic Acids Research 20, suppl (1992): 2207. http://dx.doi.org/10.1093/nar/20.suppl.2207.

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7

Issa, Amani, Florence Schlotter, Justine Flayac, et al. "The nucleolar phase of signal recognition particle assembly." Life Science Alliance 7, no. 8 (2024): e202402614. http://dx.doi.org/10.26508/lsa.202402614.

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The signal recognition particle is essential for targeting transmembrane and secreted proteins to the endoplasmic reticulum. Remarkably, because they work together in the cytoplasm, the SRP and ribosomes are assembled in the same biomolecular condensate: the nucleolus. How important is the nucleolus for SRP assembly is not known. Using quantitative proteomics, we have investigated the interactomes of SRP components. We reveal that SRP proteins are associated with scores of nucleolar proteins important for ribosome biogenesis and nucleolar structure. Having monitored the subcellular distributio

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8

Zwieb, Christian, and Jerry Eichler. "Getting on target: The archaeal signal recognition particle." Archaea 1, no. 1 (2002): 27–34. http://dx.doi.org/10.1155/2002/729649.

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Protein translocation begins with the efficient targeting of secreted and membrane proteins to complexes embedded within the membrane. In Eukarya and Bacteria, this is achieved through the interaction of the signal recognition particle (SRP) with the nascent polypeptide chain. In Archaea, homologs of eukaryal and bacterial SRP-mediated translocation pathway components have been identified. Biochemical analysis has revealed that although the archaeal system incorporates various facets of the eukaryal and bacterial targeting systems, numerous aspects of the archaeal system are unique to this dom

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9

R�misch, Karin, V�ronique Ribes, Stephen High, Henrich L�tcke, David Tollervey, and Bernhard Dobberstein. "Structure and function of signal recognition particle (SRP)." Molecular Biology Reports 14, no. 2-3 (1990): 71–72. http://dx.doi.org/10.1007/bf00360420.

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10

L�tcke, Henrich, and Bernhard Dobberstein. "Structure and function of Signal Recognition Particle (SRP)." Molecular Biology Reports 18, no. 2 (1993): 143–47. http://dx.doi.org/10.1007/bf00986769.

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11

Rapiejko, P. J., and R. Gilmore. "Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP." Molecular Biology of the Cell 5, no. 8 (1994): 887–97. http://dx.doi.org/10.1091/mbc.5.8.887.

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The identification of GTP-binding sites in the 54-kDa subunit of the signal recognition particle (SRP) and in both the alpha and beta subunits of the SRP receptor has complicated the task of defining the step in the protein translocation reaction that is controlled by the GTP-binding site in the SRP. Ribonucleotide binding assays show that the purified SRP can bind GDP or GTP. However, crosslinking experiments show that SRP54 can recognize the signal sequence of a nascent polypeptide in the absence of GTP. Targeting of SRP-ribosome-nascent polypeptide complexes, formed in the absence of GTP, t

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12

Wild, Klemens, Matthias M. M. Becker, Georg Kempf, and Irmgard Sinning. "Structure, dynamics and interactions of large SRP variants." Biological Chemistry 401, no. 1 (2019): 63–80. http://dx.doi.org/10.1515/hsz-2019-0282.

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Abstract Co-translational protein targeting to membranes relies on the signal recognition particle (SRP) system consisting of a cytosolic ribonucleoprotein complex and its membrane-associated receptor. SRP recognizes N-terminal cleavable signals or signal anchor sequences, retards translation, and delivers ribosome-nascent chain complexes (RNCs) to vacant translocation channels in the target membrane. While our mechanistic understanding is well advanced for the small bacterial systems it lags behind for the large bacterial, archaeal and eukaryotic SRP variants including an Alu and an S domain.

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13

Jomaa, Ahmad, Martin Gamerdinger, Hao-Hsuan Hsieh, et al. "Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting." Science 375, no. 6583 (2022): 839–44. http://dx.doi.org/10.1126/science.abl6459.

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The nascent polypeptide–associated complex (NAC) interacts with newly synthesized proteins at the ribosomal tunnel exit and competes with the signal recognition particle (SRP) to prevent mistargeting of cytosolic and mitochondrial polypeptides to the endoplasmic reticulum (ER). How NAC antagonizes SRP and how this is overcome by ER targeting signals are unknown. Here, we found that NAC uses two domains with opposing effects to control SRP access. The core globular domain prevented SRP from binding to signal-less ribosomes, whereas a flexibly attached domain transiently captured SRP to permit s

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14

Lee, Jae Ho, Sowmya Chandrasekar, SangYoon Chung, et al. "Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting." Proceedings of the National Academy of Sciences 115, no. 24 (2018): E5487—E5496. http://dx.doi.org/10.1073/pnas.1802252115.

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Signal recognition particle (SRP) is a universally conserved targeting machine that mediates the targeted delivery of ∼30% of the proteome. The molecular mechanism by which eukaryotic SRP achieves efficient and selective protein targeting remains elusive. Here, we describe quantitative analyses of completely reconstituted human SRP (hSRP) and SRP receptor (SR). Enzymatic and fluorescence analyses showed that the ribosome, together with a functional signal sequence on the nascent polypeptide, are required to activate SRP for rapid recruitment of the SR, thereby delivering translating ribosomes

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15

Rosch, Jason W., Luis Alberto Vega, John M. Beyer, Ada Lin, and Michael G. Caparon. "The Signal Recognition Particle Pathway Is Required for Virulence in Streptococcus pyogenes." Infection and Immunity 76, no. 6 (2008): 2612–19. http://dx.doi.org/10.1128/iai.00239-07.

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ABSTRACT The signal recognition particle (SRP) pathway is a universally conserved pathway for targeting polypeptides for secretion via the cotranslational pathway. In particular, the SRP pathway is thought to be the main mechanism for targeting polypeptides in gram-positive bacteria, including a number of important human pathogens. Though widely considered to be an essential cellular component, recent advances have indicated this pathway may be dispensable in gram-positive bacteria of the genus Streptococcus under in vitro conditions. However, its importance for the pathogenesis of streptococc

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16

Zopf, D., H. D. Bernstein, and P. Walter. "GTPase domain of the 54-kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding." Journal of Cell Biology 120, no. 5 (1993): 1113–21. http://dx.doi.org/10.1083/jcb.120.5.1113.

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The 54-kD subunit of the signal recognition particle (SRP54) binds to signal sequences of nascent secretory and transmembrane proteins. SRP54 consists of two separable domains, a 33-kD amino-terminal domain that contains a GTP-binding site (SRP54G) and a 22-kD carboxy-terminal domain (SRP54M) containing binding sites for both the signal sequence and SRP RNA. To examine the function of the two domains in more detail, we have purified SRP54M and used it to assemble a partial SRP that lacks the amino-terminal domain of SRP54 [SRP(-54G)]. This particle recognized signal sequences in two independen

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17

Dobberstein, Bernhard. "Structure and function of the signal recognition particle (SRP)." Molecular Biology Reports 12, no. 3 (1987): 213–17. http://dx.doi.org/10.1007/bf00356908.

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18

Wang, Connie Y., and Thomas F. Miller. "Allosteric Response and Substrate Sensitivity in Peptide Binding of the Signal Recognition Particle." Journal of Biological Chemistry 289, no. 44 (2014): 30868–79. http://dx.doi.org/10.1074/jbc.m114.584912.

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We characterize the conformational dynamics and substrate selectivity of the signal recognition particle (SRP) using a thermodynamic free energy cycle approach and microsecond timescale molecular dynamics simulations. The SRP is a central component of the co-translational protein targeting machinery that binds to the N-terminal signal peptide (SP) of nascent proteins. We determined the shift in relative conformational stability of the SRP upon substrate binding to quantify allosteric coupling between SRP domains. In particular, for dipeptidyl aminopeptidase, an SP that is recognized by the SRP

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19

Wolin, S. L., and P. Walter. "Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate." Journal of Cell Biology 109, no. 6 (1989): 2617–22. http://dx.doi.org/10.1083/jcb.109.6.2617.

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Signal recognition particle (SRP) is a ribonucleoprotein that functions in the targeting of ribosomes synthesizing presecretory proteins to the ER. SRP binds to the signal sequence as it emerges from the ribosome, and in wheat germ extracts, arrests further elongation. The translation arrest is released when SRP interacts with its receptor on the ER membrane. We show that the delay of elongation mediated by SRP is not unique to wheat germ translation extracts. Addition of mammalian SRP to reticulocyte lysates resulted in a delay of preprolactin synthesis due to increased ribosome pausing at sp

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20

Mainprize, Iain L., Daniel R. Beniac, Elena Falkovskaia, et al. "The Structure of Escherichia coli Signal Recognition Particle Revealed by Scanning Transmission Electron Microscopy." Molecular Biology of the Cell 17, no. 12 (2006): 5063–74. http://dx.doi.org/10.1091/mbc.e06-05-0384.

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Structural studies on various domains of the ribonucleoprotein signal recognition particle (SRP) have not converged on a single complete structure of bacterial SRP consistent with the biochemistry of the particle. We obtained a three-dimensional structure for Escherichia coli SRP by cryoscanning transmission electron microscopy and mapped the internal RNA by electron spectroscopic imaging. Crystallographic data were fit into the SRP reconstruction, and although the resulting model differed from previous models, they could be rationalized by movement through an interdomain linker of Ffh, the pr

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21

Huber, Damon, Dana Boyd, Yu Xia, Michael H. Olma, Mark Gerstein, and Jon Beckwith. "Use of Thioredoxin as a Reporter To Identify a Subset of Escherichia coli Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation." Journal of Bacteriology 187, no. 9 (2005): 2983–91. http://dx.doi.org/10.1128/jb.187.9.2983-2991.2005.

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ABSTRACT We have previously reported that the DsbA signal sequence promotes efficient, cotranslational translocation of the cytoplasmic protein thioredoxin-1 via the bacterial signal recognition particle (SRP) pathway. However, two commonly used signal sequences, those of PhoA and MalE, which promote export by a posttranslational mechanism, do not export thioredoxin. We proposed that this difference in efficiency of export was due to the rapid folding of thioredoxin in the cytoplasm; cotranslational export by the DsbA signal sequence avoids the problem of cytoplasmic folding (C. F. Schierle, M

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22

Lütcke, H., S. Prehn, A. J. Ashford, M. Remus, R. Frank, and B. Dobberstein. "Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNA." Journal of Cell Biology 121, no. 5 (1993): 977–85. http://dx.doi.org/10.1083/jcb.121.5.977.

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Signal recognition particle (SRP), the cytoplasmic ribonucleoprotein particle that mediates the targeting of proteins to the ER, consists of a 7S RNA and six different proteins. The 68- (SRP68) and 72- (SRP72) kD proteins of SRP are bound to the 7S RNA of SRP as a heterodimeric complex (SRP68/72). Here we describe the primary structure of SRP72 and the assembly of SRP68, SRP72 and 7S RNA into a ribonucleoprotein particle. The amino acid sequence deduced from the cDNA of SRP72 reveals a basic protein of 671 amino acids which shares no sequence similarity with any protein in the sequence data li

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23

Wild, Klemens, Gert Bange, Gunes Bozkurt, Bernd Segnitz, Astrid Hendricks, and Irmgard Sinning. "Structural insights into the assembly of the human and archaeal signal recognition particles." Acta Crystallographica Section D Biological Crystallography 66, no. 3 (2010): 295–303. http://dx.doi.org/10.1107/s0907444910000879.

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The signal recognition particle (SRP) is a conserved ribonucleoprotein (RNP) complex that co-translationally targets membrane and secretory proteins to membranes. The assembly of the particle depends on the proper folding of the SRP RNA, which in mammalia and archaea involves an induced-fit mechanism within helices 6 and 8 in the S domain of SRP. The two helices are juxtaposed and clamped together upon binding of the SRP19 protein to their apices. In the current assembly paradigm, archaeal SRP19 causes the asymmetric loop of helix 8 to bulge out and expose the binding platform for the key play

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24

Bradshaw, Niels, and Peter Walter. "The Signal Recognition Particle (SRP) RNA Links Conformational Changes in the SRP to Protein Targeting." Molecular Biology of the Cell 18, no. 7 (2007): 2728–34. http://dx.doi.org/10.1091/mbc.e07-02-0117.

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The RNA component of the signal recognition particle (SRP) is universally required for cotranslational protein targeting. Biochemical studies have shown that SRP RNA participates in the central step of protein targeting by catalyzing the interaction of the SRP with the SRP receptor (SR). SRP RNA also accelerates GTP hydrolysis in the SRP·SR complex once formed. Using a reverse-genetic and biochemical analysis, we identified mutations in the E. coli SRP protein, Ffh, that abrogate the activity of the SRP RNA and cause corresponding targeting defects in vivo. The mutations in Ffh that disrupt SR

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Bürk, Jonas, Benjamin Weiche, Meike Wenk, et al. "Depletion of the Signal Recognition Particle Receptor Inactivates Ribosomes in Escherichia coli." Journal of Bacteriology 191, no. 22 (2009): 7017–26. http://dx.doi.org/10.1128/jb.00208-09.

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ABSTRACT The signal recognition particle (SRP)-dependent cotranslational targeting of proteins to the cytoplasmic membrane in bacteria or the endoplasmic reticulum membrane in eukaryotes is an essential process in most living organisms. Eukaryotic cells have been shown to respond to an impairment of the SRP pathway by (i) repressing ribosome biogenesis, resulting in decreased protein synthesis, and (ii) by increasing the expression of protein quality control mechanisms, such as chaperones and proteases. In the current study, we have analyzed how bacteria like Escherichia coli respond to a grad

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26

Lam, Vinh Q., David Akopian, Michael Rome, Doug Henningsen, and Shu-ou Shan. "Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting." Journal of Cell Biology 190, no. 4 (2010): 623–35. http://dx.doi.org/10.1083/jcb.201004129.

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The signal recognition particle (SRP) and SRP receptor comprise the major cellular machinery that mediates the cotranslational targeting of proteins to cellular membranes. It remains unclear how the delivery of cargos to the target membrane is spatially coordinated. We show here that phospholipid binding drives important conformational rearrangements that activate the bacterial SRP receptor FtsY and the SRP–FtsY complex. This leads to accelerated SRP–FtsY complex assembly, and allows the SRP–FtsY complex to more efficiently unload cargo proteins. Likewise, formation of an active SRP–FtsY GTPas

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27

Neuhof, Andrea, Melissa M. Rolls, Berit Jungnickel, Kai-Uwe Kalies, and Tom A. Rapoport. "Binding of Signal Recognition Particle Gives Ribosome/Nascent Chain Complexes a Competitive Advantage in Endoplasmic Reticulum Membrane Interaction." Molecular Biology of the Cell 9, no. 1 (1998): 103–15. http://dx.doi.org/10.1091/mbc.9.1.103.

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Most secretory and membrane proteins are sorted by signal sequences to the endoplasmic reticulum (ER) membrane early during their synthesis. Targeting of the ribosome-nascent chain complex (RNC) involves the binding of the signal sequence to the signal recognition particle (SRP), followed by an interaction of ribosome-bound SRP with the SRP receptor. However, ribosomes can also independently bind to the ER translocation channel formed by the Sec61p complex. To explain the specificity of membrane targeting, it has therefore been proposed that nascent polypeptide-associated complex functions as

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Bernstein, Harris D., and Janine B. Hyndman. "Physiological Basis for Conservation of the Signal Recognition Particle Targeting Pathway in Escherichia coli." Journal of Bacteriology 183, no. 7 (2001): 2187–97. http://dx.doi.org/10.1128/jb.183.7.2187-2197.2001.

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ABSTRACT The Escherichia coli signal recognition particle (SRP) is a ribonucleoprotein complex that targets nascent inner membrane proteins (IMPs) to transport sites in the inner membrane (IM). Since SRP depletion only partially inhibits IMP insertion under some growth conditions, however, it is not clear why the particle is absolutely essential for viability. Insights into this question emerged from experiments in which we analyzed the physiological consequences of reducing the intracellular concentration of SRP below the wild-type level. We found that even moderate SRP deficiencies that have

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Pyrih, Jan, Tomáš Pánek, Ignacio Miguel Durante, et al. "Vestiges of the Bacterial Signal Recognition Particle-Based Protein Targeting in Mitochondria." Molecular Biology and Evolution 38, no. 8 (2021): 3170–87. http://dx.doi.org/10.1093/molbev/msab090.

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Abstract The main bacterial pathway for inserting proteins into the plasma membrane relies on the signal recognition particle (SRP), composed of the Ffh protein and an associated RNA component, and the SRP-docking protein FtsY. Eukaryotes use an equivalent system of archaeal origin to deliver proteins into the endoplasmic reticulum, whereas a bacteria-derived SRP and FtsY function in the plastid. Here we report on the presence of homologs of the bacterial Ffh and FtsY proteins in various unrelated plastid-lacking unicellular eukaryotes, namely Heterolobosea, Alveida, Goniomonas, and Hemimastig

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Tajima, S., L. Lauffer, V. L. Rath, and P. Walter. "The signal recognition particle receptor is a complex that contains two distinct polypeptide chains." Journal of Cell Biology 103, no. 4 (1986): 1167–78. http://dx.doi.org/10.1083/jcb.103.4.1167.

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Signal recognition particle (SRP) and SRP receptor are known to be essential components of the cellular machinery that targets nascent secretory proteins to the endoplasmic reticulum (ER) membrane. Here we report that the SRP receptor contains, in addition to the previously identified and sequenced 69-kD polypeptide (alpha-subunit, SR alpha), a 30-kD beta-subunit (SR beta). When SRP receptor was purified by SRP-Sepharose affinity chromatography, we observed the co-purification of two other ER membrane proteins. Both proteins are approximately 30 kD in size and are immunologically distinct from

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Ghosh, Sudipta, Snehlata Saini, and Ishu Saraogi. "Peptide nucleic acid mediated inhibition of the bacterial signal recognition particle." Chemical Communications 54, no. 59 (2018): 8257–60. http://dx.doi.org/10.1039/c8cc04715d.

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Palacín, Arantxa, Ricardo de la Fuente, Inmaculada Valle, Luis A. Rivas, and Rafael P. Mellado. "Streptomyces lividans contains a minimal functional signal recognition particle that is involved in protein secretion." Microbiology 149, no. 9 (2003): 2435–42. http://dx.doi.org/10.1099/mic.0.26313-0.

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The bacterial version of the mammalian signal recognition particle (SRP) is well conserved and essential to all known bacteria. The genes for the Streptomyces lividans SRP components have been cloned and characterized. FtsY resembles the mammalian SRP receptor and the S. lividans SRP consists of Ffh, a homologue of the mammalian SRP54 protein, and scRNA, which is a small size RNA of 82 nt in length. Co-immunoprecipitation studies confirmed that Ffh and scRNA are probably the only components of the S. lividans SRP and that pre-agarase can co-immunoprecipitate with Ffh, suggesting that the SRP i

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Lutcke, Henrich. "Signal Recognition Particle (SRP), a Ubiquitous Initiator of Protein Translocation." European Journal of Biochemistry 228, no. 3 (1995): 531–50. http://dx.doi.org/10.1111/j.1432-1033.1995.tb20293.x.

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Sinning, Irmgard. "Mechanisms of membrane protein biogenesis." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1161. http://dx.doi.org/10.1107/s205327331408838x.

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More than 25% of the cellular proteome comprise membrane proteins that have to be inserted into the correct target membrane. Most membrane proteins are delivered to the membrane by the signal recognition particle (SRP) pathway which relies on the recognition of an N-terminal signal sequence. In contrast to this co-translational mechanism, which avoids problems due to the hydrophobic nature of the cargo proteins, tail-anchored (TA) membrane proteins utilize a post-translational mechanism for membrane insertion – the GET pathway (guided entry of tail-anchored membrane proteins). The SRP and GET

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Okada, N., T. Mimori, R. Mukai, H. Kashiwagi, and J. A. Hardin. "Characterization of human autoantibodies that selectively precipitate the 7SL RNA component of the signal recognition particle." Journal of Immunology 138, no. 10 (1987): 3219–23. http://dx.doi.org/10.4049/jimmunol.138.10.3219.

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Abstract The signal recognition particle (SRP), which consists of the 7SL RNA molecule associated with six polypeptides ranging between 9,000 and 72,000 m.w., mediates the translocation of newly synthesized proteins across the endoplasmic reticulum. We have characterized autoantibodies that are directed against this particle from two patients with rheumatic diseases. These sera immunoprecipitated the 7SL RNA from whole extracts of HeLa cells radiolabeled with 32P, but no RNA from deproteinized cell extracts. From 35S-methionine-labeled cell extracts, they immunoprecipitated a single polypeptid

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Hwang Fu, Yu-Hsien, Sowmya Chandrasekar, Jae Ho Lee, and Shu-ou Shan. "A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting." Journal of Cell Biology 218, no. 10 (2019): 3307–19. http://dx.doi.org/10.1083/jcb.201901001.

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Molecular recognition features (MoRFs) provide interaction motifs in intrinsically disordered protein regions to mediate diverse cellular functions. Here we report that a MoRF element, located in the disordered linker domain of the mammalian signal recognition particle (SRP) receptor and conserved among eukaryotes, plays an essential role in sensing the ribosome during cotranslational protein targeting to the endoplasmic reticulum. Loss of the MoRF in the SRP receptor (SR) largely abolishes the ability of the ribosome to activate SRP-SR assembly and impairs cotranslational protein targeting. T

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He, X. P., N. Bataille, and H. M. Fried. "Nuclear export of signal recognition particle RNA is a facilitated process that involves the Alu sequence domain." Journal of Cell Science 107, no. 4 (1994): 903–12. http://dx.doi.org/10.1242/jcs.107.4.903.

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The signal recognition particle is a cytoplasmic RNA-protein complex that mediates translocation of secretory polypeptides into the endoplasmic reticulum. We have used a Xenopus oocyte microinjection assay to determine how signal recognition particle (SRP) RNA is exported from the nucleus. Following nuclear injection, SRP RNA accumulated in the cytoplasm while cytoplasmically injected SRP RNA did not enter the nucleus. Cytoplasmic accumulation of SRP RNA was an apparently facilitated process dependent on limiting trans-acting factors, since nuclear export exhibited saturation kinetics and was

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Kuhn, Patrick, Albena Draycheva, Andreas Vogt, et al. "Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon." Journal of Cell Biology 211, no. 1 (2015): 91–104. http://dx.doi.org/10.1083/jcb.201502103.

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Cotranslational protein targeting delivers proteins to the bacterial cytoplasmic membrane or to the eukaryotic endoplasmic reticulum membrane. The signal recognition particle (SRP) binds to signal sequences emerging from the ribosomal tunnel and targets the ribosome-nascent-chain complex (RNC) to the SRP receptor, termed FtsY in bacteria. FtsY interacts with the fifth cytosolic loop of SecY in the SecYEG translocon, but the functional role of the interaction is unclear. By using photo-cross-linking and fluorescence resonance energy transfer measurements, we show that FtsY–SecY complex formatio

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Shan, Shu-ou, Sandra L. Schmid, and Xin Zhang. "Signal Recognition Particle (SRP) and SRP Receptor: A New Paradigm for Multistate Regulatory GTPases." Biochemistry 48, no. 29 (2009): 6696–704. http://dx.doi.org/10.1021/bi9006989.

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Ogg, S. C., M. A. Poritz, and P. Walter. "Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae." Molecular Biology of the Cell 3, no. 8 (1992): 895–911. http://dx.doi.org/10.1091/mbc.3.8.895.

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In mammalian cells, the signal recognition particle (SRP) receptor is required for the targeting of nascent secretory proteins to the endoplasmic reticulum (ER) membrane. We have identified the Saccharomyces cerevisiae homologue of the alpha-subunit of the SRP receptor (SR alpha) and characterized its function in vivo. S. cerevisiae SR alpha is a 69-kDa peripheral membrane protein that is 32% identical (54% chemically similar) to its mammalian homologue and, like mammalian SR alpha, is predicted to contain a GTP binding domain. Yeast cells that contain the SR alpha gene (SRP101) under control

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Saraogi, Ishu, David Akopian, and Shu-ou Shan. "Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting." Journal of Cell Biology 205, no. 5 (2014): 693–706. http://dx.doi.org/10.1083/jcb.201311028.

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Efficient and accurate protein localization is essential to cells and requires protein-targeting machineries to both effectively capture the cargo in the cytosol and productively unload the cargo at the membrane. To understand how these challenges are met, we followed the interaction of translating ribosomes during their targeting by the signal recognition particle (SRP) using a site-specific fluorescent probe in the nascent protein. We show that initial recruitment of SRP receptor (SR) selectively enhances the affinity of SRP for correct cargos, thus committing SRP-dependent substrates to the

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Wiedmann, M., T. V. Kurzchalia, H. Bielka, and T. A. Rapoport. "Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking." Journal of Cell Biology 104, no. 2 (1987): 201–8. http://dx.doi.org/10.1083/jcb.104.2.201.

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We have studied the interaction between the signal sequence of nascent preprolactin and the signal recognition particle (SRP) during the initial events in protein translocation across the endoplasmic reticulum membrane. A new method of affinity labeling was used, whereby lysine residues, carrying the photoreactive group 4-(3-trifluoromethyldiazirino) benzoic acid in their side chains, are incorporated into a protein by means of modified lysyl-tRNA, and cross-linking to the interacting component is induced by irradiation. SRP interacts through its Mr 54,000 polypeptide component with the signal

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Andrews, D. W., L. Lauffer, P. Walter, and V. R. Lingappa. "Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor." Journal of Cell Biology 108, no. 3 (1989): 797–810. http://dx.doi.org/10.1083/jcb.108.3.797.

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The signal recognition particle (SRP) and SRP receptor act sequentially to target nascent secretory proteins to the membrane of the ER. The SRP receptor consists of two subunits, SR alpha and SR beta, both tightly associated with the ER membrane. To examine the biogenesis of the SRP receptor we have developed a cell-free assay system that reconstitutes SR alpha membrane assembly and permits both anchoring and functional properties to be assayed independently. Our experiments reveal a mechanism involving at least two distinct steps, targeting to the ER and anchoring of the targeted molecule on

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Wang, Huping, and Ramanujan S. Hegde. "Identification of a factor that accelerates substrate release from the signal recognition particle." Science 386, no. 6725 (2024): 996–1003. http://dx.doi.org/10.1126/science.adp0787.

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The eukaryotic signal recognition particle (SRP) cotranslationally recognizes the first hydrophobic segment of nascent secretory and membrane proteins and delivers them to a receptor at the endoplasmic reticulum (ER). How substrates are released from SRP at the ER to subsequently access translocation factors is not well understood. We found that TMEM208 can engage the substrate binding domain of SRP to accelerate release of its bound cargo. Without TMEM208, slow cargo release resulted in excessive synthesis of downstream polypeptide before engaging translocation factors. Delayed access to tran

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Bacher, Gerald, Martin Pool та Bernhard Dobberstein. "The Ribosome Regulates the Gtpase of the β-Subunit of the Signal Recognition Particle Receptor". Journal of Cell Biology 146, № 4 (1999): 723–30. http://dx.doi.org/10.1083/jcb.146.4.723.

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Protein targeting to the membrane of the ER is regulated by three GTPases, the 54-kD subunit of the signal recognition particle (SRP) and the α- and β-subunit of the SRP receptor (SR). Here, we report on the GTPase cycle of the β-subunits of the SR (SRβ). We found that SRβ binds GTP with high affinity and interacts with ribosomes in the GTP-bound state. Subsequently, the ribosome increases the GTPase activity of SRβ and thus functions as a GTPase activating protein for SRβ. Furthermore, the interaction between SRβ and the ribosome leads to a reduction in the affinity of SRβ for guanine nucleot

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Ren, Yan-Guo, Klaus W. Wagner, Deborah A. Knee, Pedro Aza-Blanc, Marc Nasoff, and Quinn L. Deveraux. "Differential Regulation of the TRAIL Death Receptors DR4 and DR5 by the Signal Recognition Particle." Molecular Biology of the Cell 15, no. 11 (2004): 5064–74. http://dx.doi.org/10.1091/mbc.e04-03-0184.

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TRAIL (TNF-related apoptosis-inducing ligand) death receptors DR4 and DR5 facilitate the selective elimination of malignant cells through the induction of apoptosis. From previous studies the regulation of the DR4 and DR5 cell-death pathways appeared similar; nevertheless in this study we screened a library of small interfering RNA (siRNA) for genes, which when silenced, differentially affect DR4- vs. DR5-mediated apoptosis. These experiments revealed that expression of the signal recognition particle (SRP) complex is essential for apoptosis mediated by DR4, but not DR5. Selective diminution o

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Du, Ying, and Cindy Grove Arvidson. "Identification of ZipA, a Signal Recognition Particle-Dependent Protein from Neisseria gonorrhoeae." Journal of Bacteriology 185, no. 7 (2003): 2122–30. http://dx.doi.org/10.1128/jb.185.7.2122-2130.2003.

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ABSTRACT A genetic screen designed to identify proteins that utilize the signal recognition particle (SRP) for targeting in Escherichia coli was used to screen a Neisseria gonorrhoeae plasmid library. Six plasmids were identified in this screen, and each is predicted to encode one or more putative cytoplasmic membrane (CM) proteins. One of these, pSLO7, has three open reading frames (ORFs), two of which have no similarity to known proteins in GenBank other than sequences from the closely related N. meningitidis. Further analyses showed that one of these, SLO7ORF3, encodes a protein that is dep

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Braig, David, Miryana Mircheva, Ilie Sachelaru, et al. "Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle." Molecular Biology of the Cell 22, no. 13 (2011): 2309–23. http://dx.doi.org/10.1091/mbc.e11-02-0152.

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Protein targeting by the signal recognition particle (SRP) and the bacterial SRP receptor FtsY requires a series of closely coordinated steps that monitor the presence of a substrate, the membrane, and a vacant translocon. Although the influence of substrate binding on FtsY-SRP complex formation is well documented, the contribution of the membrane is largely unknown. In the current study, we found that negatively charged phospholipids stimulate FtsY-SRP complex formation. Phospholipids act on a conserved positively charged amphipathic helix in FtsY and induce a conformational change that stron

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Bowers, Christina Wilson, Fion Lau, and Thomas J. Silhavy. "Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coli." Journal of Bacteriology 185, no. 19 (2003): 5697–705. http://dx.doi.org/10.1128/jb.185.19.5697-5705.2003.

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ABSTRACT LamB-LacZ fusion proteins have classically been used in studies of the general secretion pathway of Escherichia coli. Here we describe how increasing signal sequence hydrophobicity routes LamB-LacZ Hyb42-1 to the signal recognition particle (SRP) pathway. Secretion of this hydrophobic fusion variant (H*LamB-LacZ) was reduced in the absence of fully functional Ffh and Ffs, and the translocator jamming caused by Hyb42-1 was prevented by efficient delivery of the fusion to the periplasm. Finally, we found that in the absence of the ribosome-associated chaperone, trigger factor (Tig), Lam

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Rose, R. Wesley, and Mechthild Pohlschröder. "In Vivo Analysis of an Essential Archaeal Signal Recognition Particle in Its Native Host." Journal of Bacteriology 184, no. 12 (2002): 3260–67. http://dx.doi.org/10.1128/jb.184.12.3260-3267.2002.

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ABSTRACT The evolutionarily conserved signal recognition particle (SRP) plays an integral role in Sec-mediated cotranslational protein translocation and membrane protein insertion, as it has been shown to target nascent secretory and membrane proteins to the bacterial and eukaryotic translocation pores. However, little is known about its function in archaea, since characterization of the SRP in this domain of life has thus far been limited to in vitro reconstitution studies of heterologously expressed archaeal SRP components identified by sequence comparisons. In the present study, the genes e

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