Literature Help
SRP68 / YPL243W Literature
All manually curated literature for the specified gene, organized by relevance to the gene and by
association with specific annotations to the gene in SGD. SGD gathers references via a PubMed search for
papers whose titles or abstracts contain “yeast” or “cerevisiae;” these papers are reviewed manually and
linked to relevant genes and literature topics by SGD curators.
Primary Literature
Literature that either focuses on the gene or contains information about function, biological role,
cellular location, phenotype, regulation, structure, or disease homologs in other species for the gene
or gene product.
No primary literature curated.
Download References (.nbib)
- Doh JH, et al. (2014) Co-translational localization of an LTR-retrotransposon RNA to the endoplasmic reticulum nucleates virus-like particle assembly sites. PLoS Genet 10(3):e1004219 PMID:24603646
- Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 PMID:22842922
- del Alamo M, et al. (2011) Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes. PLoS Biol 9(7):e1001100 PMID:21765803
- Grosshans H, et al. (2001) Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol 153(4):745-62 PMID:11352936
- Ciufo LF and Brown JD (2000) Nuclear export of yeast signal recognition particle lacking Srp54p by the Xpo1p/Crm1p NES-dependent pathway. Curr Biol 10(20):1256-64 PMID:11069106
- Mason N, et al. (2000) Elongation arrest is a physiologically important function of signal recognition particle. EMBO J 19(15):4164-74 PMID:10921896
- Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400 PMID:7925282
Related Literature
Genes that share literature (indicated by the purple circles) with the specified gene (indicated by yellow circle).
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Additional Literature
Papers that show experimental evidence for the gene or describe homologs in other species, but
for which the gene is not the paper’s principal focus.
No additional literature curated.
Download References (.nbib)
- Dublin-Ryan LB, et al. (2024) Disruption of the nascent polypeptide-associated complex leads to reduced polyglutamine aggregation and toxicity. PLoS One 19(8):e0303008 PMID:39146256
- Lanz MC, et al. (2021) In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Rep 22(2):e51121 PMID:33491328
- Weill U, et al. (2019) Assessment of GFP Tag Position on Protein Localization and Growth Fitness in Yeast. J Mol Biol 431(3):636-641 PMID:30550779
- Costa EA, et al. (2018) Defining the physiological role of SRP in protein-targeting efficiency and specificity. Science 359(6376):689-692 PMID:29348368
- Chartron JW, et al. (2016) Cotranslational signal-independent SRP preloading during membrane targeting. Nature 536(7615):224-8 PMID:27487213
- Gallego O, et al. (2010) A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol 6:430 PMID:21119626
- Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8 PMID:18622397
- Dalley JA, et al. (2008) Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation. Mol Biol Cell 19(7):2876-84 PMID:18448667
- Altmann K and Westermann B (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410-7 PMID:16135527
- Willer M, et al. (2003) An in vitro assay using overexpressed yeast SRP demonstrates that cotranslational translocation is dependent upon the J-domain of Sec63p. Biochemistry 42(23):7171-7 PMID:12795613
Reviews
No reviews curated.
Download References (.nbib)
- Luo Y, et al. (2025) Mechanism and engineering of endoplasmic reticulum-localized membrane protein folding in Saccharomyces cerevisiae. Metab Eng 90:43-56 PMID:40064436
- Gamerdinger M and Deuerling E (2024) Cotranslational sorting and processing of newly synthesized proteins in eukaryotes. Trends Biochem Sci 49(2):105-118 PMID:37919225
- Pool MR (2022) Targeting of Proteins for Translocation at the Endoplasmic Reticulum. Int J Mol Sci 23(7) PMID:35409131
- Barlowe CK and Miller EA (2013) Secretory protein biogenesis and traffic in the early secretory pathway. Genetics 193(2):383-410 PMID:23396477
- Hou J, et al. (2012) Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae. FEMS Yeast Res 12(5):491-510 PMID:22533807
- Zimmermann R, et al. (2011) Protein translocation across the ER membrane. Biochim Biophys Acta 1808(3):912-24 PMID:20599535
- Fonzi WA (2009) The protein secretory pathway of Candida albicans. Mycoses 52(4):291-303 PMID:19207839
- Pool MR (2005) Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review). Mol Membr Biol 22(1-2):3-15 PMID:16092520
- Agarraberes FA and Dice JF (2001) Protein translocation across membranes. Biochim Biophys Acta 1513(1):1-24 PMID:11427190
- Lewis JD and Tollervey D (2000) Like attracts like: getting RNA processing together in the nucleus. Science 288(5470):1385-9 PMID:10827942
Gene Ontology Literature
Paper(s) associated with one or more GO (Gene Ontology) terms in SGD for the specified gene.
No gene ontology literature curated.
Download References (.nbib)
- Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 PMID:22842922
- Mason N, et al. (2000) Elongation arrest is a physiologically important function of signal recognition particle. EMBO J 19(15):4164-74 PMID:10921896
- Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400 PMID:7925282
Phenotype Literature
Paper(s) associated with one or more pieces of classical phenotype evidence in SGD for the specified gene.
No phenotype literature curated.
Download References (.nbib)
- Grosshans H, et al. (2001) Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol 153(4):745-62 PMID:11352936
- Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400 PMID:7925282
Interaction Literature
Paper(s) associated with evidence supporting a physical or genetic interaction between the
specified gene and another gene in SGD. Currently, all interaction evidence is obtained from
BioGRID.
No interaction literature curated.
Download References (.nbib)
- Marmorale LJ, et al. (2024) Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking. J Cell Biol 223(3) PMID:38240799
- O'Brien MJ and Ansari A (2024) Protein interaction network revealed by quantitative proteomic analysis links TFIIB to multiple aspects of the transcription cycle. Biochim Biophys Acta Proteins Proteom 1872(1):140968 PMID:37863410
- Yeter-Alat H, et al. (2024) The RNA Helicase Ded1 from Yeast Is Associated with the Signal Recognition Particle and Is Regulated by SRP21. Molecules 29(12) PMID:38931009
- Ali A, et al. (2023) Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates. Nat Cell Biol 25(11):1691-1703 PMID:37845327
- Cohen N, et al. (2023) A systematic proximity ligation approach to studying protein-substrate specificity identifies the substrate spectrum of the Ssh1 translocon. EMBO J 42(11):e113385 PMID:37073826
- Michaelis AC, et al. (2023) The social and structural architecture of the yeast protein interactome. Nature 624(7990):192-200 PMID:37968396
- Gavade JN, et al. (2022) Identification of 14-3-3 proteins, Polo kinase, and RNA-binding protein Pes4 as key regulators of meiotic commitment in budding yeast. Curr Biol 32(7):1534-1547.e9 PMID:35240051
- Mattingly M, et al. (2022) Mediator recruits the cohesin loader Scc2 to RNA Pol II-transcribed genes and promotes sister chromatid cohesion. Curr Biol 32(13):2884-2896.e6 PMID:35654035
- Perica T, et al. (2021) Systems-level effects of allosteric perturbations to a model molecular switch. Nature 599(7883):152-157 PMID:34646016
- Schoppe J, et al. (2020) AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering. EMBO J 39(20):e105117 PMID:32840906
- Pereira F, et al. (2019) Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation. PLoS One 14(1):e0211180 PMID:30682149
- Rössler I, et al. (2019) Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME. Nucleic Acids Res 47(13):6984-7002 PMID:31062022
- Gay S, et al. (2018) A Mad2-Mediated Translational Regulatory Mechanism Promoting S-Phase Cyclin Synthesis Controls Origin Firing and Survival to Replication Stress. Mol Cell 70(4):628-638.e5 PMID:29775579
- Miller JE, et al. (2018) Genome-Wide Mapping of Decay Factor-mRNA Interactions in Yeast Identifies Nutrient-Responsive Transcripts as Targets of the Deadenylase Ccr4. G3 (Bethesda) 8(1):315-330 PMID:29158339
- Jungfleisch J, et al. (2017) A novel translational control mechanism involving RNA structures within coding sequences. Genome Res 27(1):95-106 PMID:27821408
- Lapointe CP, et al. (2017) Architecture and dynamics of overlapped RNA regulatory networks. RNA 23(11):1636-1647 PMID:28768715
- Buser R, et al. (2016) The Replisome-Coupled E3 Ubiquitin Ligase Rtt101Mms22 Counteracts Mrc1 Function to Tolerate Genotoxic Stress. PLoS Genet 12(2):e1005843 PMID:26849847
- Costanzo M, et al. (2016) A global genetic interaction network maps a wiring diagram of cellular function. Science 353(6306) PMID:27708008
- Kershaw CJ, et al. (2015) Integrated multi-omics analyses reveal the pleiotropic nature of the control of gene expression by Puf3p. Sci Rep 5:15518 PMID:26493364
- Kırlı K, et al. (2015) A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning. Elife 4 PMID:26673895
- Elbaz-Alon Y, et al. (2014) A dynamic interface between vacuoles and mitochondria in yeast. Dev Cell 30(1):95-102 PMID:25026036
- Rossi D, et al. (2014) eIF5A has a function in the cotranslational translocation of proteins into the ER. Amino Acids 46(3):645-53 PMID:24306454
- Freeberg MA, et al. (2013) Pervasive and dynamic protein binding sites of the mRNA transcriptome in Saccharomyces cerevisiae. Genome Biol 14(2):R13 PMID:23409723
- Mitchell SF, et al. (2013) Global analysis of yeast mRNPs. Nat Struct Mol Biol 20(1):127-33 PMID:23222640
- Srikumar T, et al. (2013) A global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome. Mol Syst Biol 9:668 PMID:23712011
- Willmund F, et al. (2013) The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell 152(1-2):196-209 PMID:23332755
- Babu M, et al. (2012) Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae. Nature 489(7417):585-9 PMID:22940862
- del Alamo M, et al. (2011) Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes. PLoS Biol 9(7):e1001100 PMID:21765803
- García-Gómez JJ, et al. (2011) Dynamics of the putative RNA helicase Spb4 during ribosome assembly in Saccharomyces cerevisiae. Mol Cell Biol 31(20):4156-64 PMID:21825077
- Ossareh-Nazari B, et al. (2010) Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy. EMBO Rep 11(7):548-54 PMID:20508643
- Batisse J, et al. (2009) Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure. J Biol Chem 284(50):34911-7 PMID:19840948
- Yu H, et al. (2008) High-quality binary protein interaction map of the yeast interactome network. Science 322(5898):104-10 PMID:18719252
- McClellan AJ, et al. (2007) Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131(1):121-35 PMID:17923092
- Gavin AC, et al. (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature 440(7084):631-6 PMID:16429126
- Krogan NJ, et al. (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440(7084):637-43 PMID:16554755
- Krogan NJ, et al. (2004) High-definition macromolecular composition of yeast RNA-processing complexes. Mol Cell 13(2):225-39 PMID:14759368
- Gavin AC, et al. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415(6868):141-7 PMID:11805826
- Mason N, et al. (2000) Elongation arrest is a physiologically important function of signal recognition particle. EMBO J 19(15):4164-74 PMID:10921896
- Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400 PMID:7925282
Regulation Literature
Paper(s) associated with one or more pieces of regulation evidence in SGD, as found on the
Regulation page.
No regulation literature curated.
Post-translational Modifications Literature
Paper(s) associated with one or more pieces of post-translational modifications evidence in SGD.
No post-translational modifications literature curated.
Download References (.nbib)
- Leutert M, et al. (2023) The regulatory landscape of the yeast phosphoproteome. Nat Struct Mol Biol 30(11):1761-1773 PMID:37845410
- Lanz MC, et al. (2021) In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Rep 22(2):e51121 PMID:33491328
- Zhou X, et al. (2021) Cross-compartment signal propagation in the mitotic exit network. Elife 10 PMID:33481703
- Swaney DL, et al. (2013) Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat Methods 10(7):676-82 PMID:23749301
- Henriksen P, et al. (2012) Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol Cell Proteomics 11(11):1510-22 PMID:22865919
High-Throughput Literature
Paper(s) associated with one or more pieces of high-throughput evidence in SGD.
No high-throughput literature curated.
Download References (.nbib)
- Forster DT, et al. (2022) BIONIC: biological network integration using convolutions. Nat Methods 19(10):1250-1261 PMID:36192463
- Doh JH, et al. (2014) Co-translational localization of an LTR-retrotransposon RNA to the endoplasmic reticulum nucleates virus-like particle assembly sites. PLoS Genet 10(3):e1004219 PMID:24603646
- Ostrow AZ, et al. (2014) Fkh1 and Fkh2 bind multiple chromosomal elements in the S. cerevisiae genome with distinct specificities and cell cycle dynamics. PLoS One 9(2):e87647 PMID:24504085
- Cheng E, et al. (2012) Genome rearrangements caused by depletion of essential DNA replication proteins in Saccharomyces cerevisiae. Genetics 192(1):147-60 PMID:22673806
- Venters BJ, et al. (2011) A comprehensive genomic binding map of gene and chromatin regulatory proteins in Saccharomyces. Mol Cell 41(4):480-92 PMID:21329885
- Dowell RD, et al. (2010) Genotype to phenotype: a complex problem. Science 328(5977):469 PMID:20413493
- Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8 PMID:18622397
- Sopko R, et al. (2006) Mapping pathways and phenotypes by systematic gene overexpression. Mol Cell 21(3):319-30 PMID:16455487
- Altmann K and Westermann B (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410-7 PMID:16135527
- Lum PY, et al. (2004) Discovering modes of action for therapeutic compounds using a genome-wide screen of yeast heterozygotes. Cell 116(1):121-37 PMID:14718172
- Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 PMID:12140549