6q8y

Structural highlights

Function

[XRN1_YEAST] Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus-like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post-transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth.^{[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35]} [RSSA1_YEAST] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.^{[36] [37]} [RL37A_YEAST] Binds to the 23S rRNA (By similarity). [RS21A_YEAST] Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.^[38] [RL40A_YEAST] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 60S ribosomal protein L40-A: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eL40 is essential for translation of a subset of cellular transcripts, including stress response transcripts, such as DDR2 (PubMed:23169626).^{[39] [40]} [RS15_YEAST] Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm.^[41] [RS27A_YEAST] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 40S ribosomal protein S31 is a component of the 40S subunit of the ribosome (By similarity). [RS9A_YEAST] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.^[42] [RS18A_YEAST] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity).[HAMAP-Rule:MF_01315] [RS14B_YEAST] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.^[43] [RS2_YEAST] Important in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.^[44] [RS7A_YEAST] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.^[45] [GBLP_YEAST] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.^[46] [RS19A_YEAST] Required for proper maturation of the small (40S) ribosomal subunit. Binds to 40s pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.^{[47] [48]} [RS6A_YEAST] Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.^[49] [RS31_YEAST] Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 40S ribosomal protein S31: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.^[50] [RL4A_YEAST] Participates in the regulation of the accumulation of its own mRNA.^[51] [RL5_YEAST] Binds 5S RNA and is required for 60S subunit assembly. [RL25_YEAST] This protein binds to a specific region on the 26S rRNA. [RL11B_YEAST] Binds to 5S ribosomal RNA.

References

1. ↑ Solinger JA, Pascolini D, Heyer WD. Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis. Mol Cell Biol. 1999 Sep;19(9):5930-42. PMID:10454540
2. ↑ Geerlings TH, Vos JC, Raue HA. The final step in the formation of 25S rRNA in Saccharomyces cerevisiae is performed by 5'-->3' exonucleases. RNA. 2000 Dec;6(12):1698-703. PMID:11142370
3. ↑ He F, Jacobson A. Upf1p, Nmd2p, and Upf3p regulate the decapping and exonucleolytic degradation of both nonsense-containing mRNAs and wild-type mRNAs. Mol Cell Biol. 2001 Mar;21(5):1515-30. PMID:11238889 doi:http://dx.doi.org/10.1128/MCB.21.5.1515-1530.2001
4. ↑ Frischmeyer PA, van Hoof A, O'Donnell K, Guerrerio AL, Parker R, Dietz HC. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science. 2002 Mar 22;295(5563):2258-61. doi: 10.1126/science.1067338. PMID:11910109 doi:http://dx.doi.org/10.1126/science.1067338
5. ↑ Kim J, Kim J. KEM1 is involved in filamentous growth of Saccharomyces cerevisiae. FEMS Microbiol Lett. 2002 Oct 29;216(1):33-8. doi:, 10.1111/j.1574-6968.2002.tb11410.x. PMID:12423748 doi:http://dx.doi.org/10.1111/j.1574-6968.2002.tb11410.x
6. ↑ Kebaara B, Nazarenus T, Taylor R, Forch A, Atkin AL. The Upf-dependent decay of wild-type PPR1 mRNA depends on its 5'-UTR and first 92 ORF nucleotides. Nucleic Acids Res. 2003 Jun 15;31(12):3157-65. PMID:12799443
7. ↑ Heikkinen HL, Llewellyn SA, Barnes CA. Initiation-mediated mRNA decay in yeast affects heat-shock mRNAs, and works through decapping and 5'-to-3' hydrolysis. Nucleic Acids Res. 2003 Jul 15;31(14):4006-16. PMID:12853617
8. ↑ Lee CY, Lee A, Chanfreau G. The roles of endonucleolytic cleavage and exonucleolytic digestion in the 5'-end processing of S. cerevisiae box C/D snoRNAs. RNA. 2003 Nov;9(11):1362-70. PMID:14561886
9. ↑ He F, Li X, Spatrick P, Casillo R, Dong S, Jacobson A. Genome-wide analysis of mRNAs regulated by the nonsense-mediated and 5' to 3' mRNA decay pathways in yeast. Mol Cell. 2003 Dec;12(6):1439-52. PMID:14690598
10. ↑ Gill T, Cai T, Aulds J, Wierzbicki S, Schmitt ME. RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation. Mol Cell Biol. 2004 Feb;24(3):945-53. PMID:14729943
11. ↑ Yano T, Inukai M, Isono F. Deletion of OSH3 gene confers resistance against ISP-1 in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 2004 Feb 27;315(1):228-34. PMID:15013450 doi:http://dx.doi.org/10.1016/j.bbrc.2004.01.039
12. ↑ Kim J, Jeon S, Yang YS, Kim J. Posttranscriptional regulation of the karyogamy gene by Kem1p/Xrn1p exoribonuclease and Rok1p RNA helicase of Saccharomyces cerevisiae. Biochem Biophys Res Commun. 2004 Sep 3;321(4):1032-9. doi:, 10.1016/j.bbrc.2004.07.065. PMID:15358132 doi:http://dx.doi.org/10.1016/j.bbrc.2004.07.065
13. ↑ Zer C, Chanfreau G. Regulation and surveillance of normal and 3'-extended forms of the yeast aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic degradation. J Biol Chem. 2005 Aug 12;280(32):28997-9003. doi: 10.1074/jbc.M505913200. Epub, 2005 Jun 20. PMID:15967792 doi:http://dx.doi.org/10.1074/jbc.M505913200
14. ↑ Lee A, Henras AK, Chanfreau G. Multiple RNA surveillance pathways limit aberrant expression of iron uptake mRNAs and prevent iron toxicity in S. cerevisiae. Mol Cell. 2005 Jul 1;19(1):39-51. doi: 10.1016/j.molcel.2005.05.021. PMID:15989963 doi:http://dx.doi.org/10.1016/j.molcel.2005.05.021
15. ↑ Pathak R, Bogomolnaya LM, Guo J, Polymenis M. A role for KEM1 at the START of the cell cycle in Saccharomyces cerevisiae. Curr Genet. 2005 Nov;48(5):300-9. doi: 10.1007/s00294-005-0030-5. Epub 2005 Nov, 4. PMID:16240118 doi:http://dx.doi.org/10.1007/s00294-005-0030-5
16. ↑ Beliakova-Bethell N, Beckham C, Giddings TH Jr, Winey M, Parker R, Sandmeyer S. Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components. RNA. 2006 Jan;12(1):94-101. doi: 10.1261/rna.2264806. PMID:16373495 doi:http://dx.doi.org/10.1261/rna.2264806
17. ↑ Cheng CP, Serviene E, Nagy PD. Suppression of viral RNA recombination by a host exoribonuclease. J Virol. 2006 Mar;80(6):2631-40. doi: 10.1128/JVI.80.6.2631-2640.2006. PMID:16501073 doi:http://dx.doi.org/10.1128/JVI.80.6.2631-2640.2006
18. ↑ Meaux S, Van Hoof A. Yeast transcripts cleaved by an internal ribozyme provide new insight into the role of the cap and poly(A) tail in translation and mRNA decay. RNA. 2006 Jul;12(7):1323-37. doi: 10.1261/rna.46306. Epub 2006 May 19. PMID:16714281 doi:http://dx.doi.org/10.1261/rna.46306
19. ↑ Jang LT, Buu LM, Lee FJ. Determinants of Rbp1p localization in specific cytoplasmic mRNA-processing foci, P-bodies. J Biol Chem. 2006 Sep 29;281(39):29379-90. doi: 10.1074/jbc.M601573200. Epub 2006, Aug 2. PMID:16885161 doi:http://dx.doi.org/10.1074/jbc.M601573200
20. ↑ Choi HS, Carman GM. Respiratory deficiency mediates the regulation of CHO1-encoded phosphatidylserine synthase by mRNA stability in Saccharomyces cerevisiae. J Biol Chem. 2007 Oct 26;282(43):31217-27. doi: 10.1074/jbc.M705098200. Epub 2007, Aug 30. PMID:17761681 doi:http://dx.doi.org/10.1074/jbc.M705098200
21. ↑ Beckham C, Hilliker A, Cziko AM, Noueiry A, Ramaswami M, Parker R. The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces cerevisiae P-bodies. Mol Biol Cell. 2008 Mar;19(3):984-93. doi: 10.1091/mbc.e07-09-0954. Epub 2007 Dec, 27. PMID:18162578 doi:http://dx.doi.org/10.1091/mbc.e07-09-0954
22. ↑ Chernyakov I, Whipple JM, Kotelawala L, Grayhack EJ, Phizicky EM. Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5'-3' exonucleases Rat1 and Xrn1. Genes Dev. 2008 May 15;22(10):1369-80. doi: 10.1101/gad.1654308. Epub 2008 Apr, 28. PMID:18443146 doi:http://dx.doi.org/10.1101/gad.1654308
23. ↑ Rendl LM, Bieman MA, Smibert CA. S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation and interacts with the Ccr4p-Pop2p-Not deadenylase complex. RNA. 2008 Jul;14(7):1328-36. doi: 10.1261/rna.955508. Epub 2008 May 9. PMID:18469165 doi:http://dx.doi.org/10.1261/rna.955508
24. ↑ Esteban R, Vega L, Fujimura T. 20S RNA narnavirus defies the antiviral activity of SKI1/XRN1 in Saccharomyces cerevisiae. J Biol Chem. 2008 Sep 19;283(38):25812-20. doi: 10.1074/jbc.M804400200. Epub 2008, Jul 18. PMID:18640978 doi:http://dx.doi.org/10.1074/jbc.M804400200
25. ↑ Goler-Baron V, Selitrennik M, Barkai O, Haimovich G, Lotan R, Choder M. Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes. Genes Dev. 2008 Aug 1;22(15):2022-7. doi: 10.1101/gad.473608. PMID:18676807 doi:http://dx.doi.org/10.1101/gad.473608
26. ↑ Pedro-Segura E, Vergara SV, Rodriguez-Navarro S, Parker R, Thiele DJ, Puig S. The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the decay of succinate dehydrogenase SDH4 mRNA in response to iron deficiency. J Biol Chem. 2008 Oct 17;283(42):28527-35. Epub 2008 Aug 20. PMID:18715869 doi:http://dx.doi.org/M804910200
27. ↑ Holbein S, Wengi A, Decourty L, Freimoser FM, Jacquier A, Dichtl B. Cordycepin interferes with 3' end formation in yeast independently of its potential to terminate RNA chain elongation. RNA. 2009 May;15(5):837-49. doi: 10.1261/rna.1458909. Epub 2009 Mar 26. PMID:19324962 doi:http://dx.doi.org/10.1261/rna.1458909
28. ↑ Kim J, Ljungdahl PO, Fink GR. kem mutations affect nuclear fusion in Saccharomyces cerevisiae. Genetics. 1990 Dec;126(4):799-812. PMID:2076815
29. ↑ Liu Z, Lee A, Gilbert W. Gene disruption of a G4-DNA-dependent nuclease in yeast leads to cellular senescence and telomere shortening. Proc Natl Acad Sci U S A. 1995 Jun 20;92(13):6002-6. PMID:7597069
30. ↑ Chen J, Kanaar R, Cozzarelli NR. The Sep1 strand exchange protein from Saccharomyces cerevisiae promotes a paranemic joint between homologous DNA molecules. Genes Dev. 1994 Jun 1;8(11):1356-66. PMID:7926736
31. ↑ Johnson AW. Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively. Mol Cell Biol. 1997 Oct;17(10):6122-30. PMID:9315672
32. ↑ Anderson JS, Parker RP. The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex. EMBO J. 1998 Mar 2;17(5):1497-506. PMID:9482746 doi:10.1093/emboj/17.5.1497
33. ↑ Petfalski E, Dandekar T, Henry Y, Tollervey D. Processing of the precursors to small nucleolar RNAs and rRNAs requires common components. Mol Cell Biol. 1998 Mar;18(3):1181-9. PMID:9488433
34. ↑ Page AM, Davis K, Molineux C, Kolodner RD, Johnson AW. Mutational analysis of exoribonuclease I from Saccharomyces cerevisiae. Nucleic Acids Res. 1998 Aug 15;26(16):3707-16. PMID:9685486
35. ↑ Lew JE, Enomoto S, Berman J. Telomere length regulation and telomeric chromatin require the nonsense-mediated mRNA decay pathway. Mol Cell Biol. 1998 Oct;18(10):6121-30. PMID:9742129
36. ↑ Ford CL, Randal-Whitis L, Ellis SR. Yeast proteins related to the p40/laminin receptor precursor are required for 20S ribosomal RNA processing and the maturation of 40S ribosomal subunits. Cancer Res. 1999 Feb 1;59(3):704-10. PMID:9973221
37. ↑ Tabb-Massey A, Caffrey JM, Logsden P, Taylor S, Trent JO, Ellis SR. Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have overlapping functions in the maturation of the 3' end of 18S rRNA. Nucleic Acids Res. 2003 Dec 1;31(23):6798-805. PMID:14627813
38. ↑ Tabb-Massey A, Caffrey JM, Logsden P, Taylor S, Trent JO, Ellis SR. Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have overlapping functions in the maturation of the 3' end of 18S rRNA. Nucleic Acids Res. 2003 Dec 1;31(23):6798-805. PMID:14627813
39. ↑ Lee AS, Burdeinick-Kerr R, Whelan SP. A ribosome-specialized translation initiation pathway is required for cap-dependent translation of vesicular stomatitis virus mRNAs. Proc Natl Acad Sci U S A. 2013 Jan 2;110(1):324-9. doi: 10.1073/pnas.1216454109. , Epub 2012 Nov 19. PMID:23169626 doi:http://dx.doi.org/10.1073/pnas.1216454109
40. ↑ Ben-Shem A, Garreau de Loubresse N, Melnikov S, Jenner L, Yusupova G, Yusupov M. The structure of the eukaryotic ribosome at 3.0 A resolution. Science. 2011 Dec 16;334(6062):1524-9. Epub 2011 Nov 17. PMID:22096102 doi:10.1126/science.1212642
41. ↑ Leger-Silvestre I, Milkereit P, Ferreira-Cerca S, Saveanu C, Rousselle JC, Choesmel V, Guinefoleau C, Gas N, Gleizes PE. The ribosomal protein Rps15p is required for nuclear exit of the 40S subunit precursors in yeast. EMBO J. 2004 Jun 16;23(12):2336-47. Epub 2004 May 27. PMID:15167894 doi:http://dx.doi.org/10.1038/sj.emboj.7600252
42. ↑ Bernstein KA, Gallagher JE, Mitchell BM, Granneman S, Baserga SJ. The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell. 2004 Dec;3(6):1619-26. PMID:15590835 doi:http://dx.doi.org/10.1128/EC.3.6.1619-1626.2004
43. ↑ Bernstein KA, Gallagher JE, Mitchell BM, Granneman S, Baserga SJ. The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell. 2004 Dec;3(6):1619-26. PMID:15590835 doi:http://dx.doi.org/10.1128/EC.3.6.1619-1626.2004
44. ↑ Bernstein KA, Gallagher JE, Mitchell BM, Granneman S, Baserga SJ. The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell. 2004 Dec;3(6):1619-26. PMID:15590835 doi:http://dx.doi.org/10.1128/EC.3.6.1619-1626.2004
45. ↑ Bernstein KA, Gallagher JE, Mitchell BM, Granneman S, Baserga SJ. The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell. 2004 Dec;3(6):1619-26. PMID:15590835 doi:http://dx.doi.org/10.1128/EC.3.6.1619-1626.2004
46. ↑ Gerbasi VR, Weaver CM, Hill S, Friedman DB, Link AJ. Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol Cell Biol. 2004 Sep;24(18):8276-87. PMID:15340087 doi:10.1128/MCB.24.18.8276-8287.2004
47. ↑ Leger-Silvestre I, Caffrey JM, Dawaliby R, Alvarez-Arias DA, Gas N, Bertolone SJ, Gleizes PE, Ellis SR. Specific Role for Yeast Homologs of the Diamond Blackfan Anemia-associated Rps19 Protein in Ribosome Synthesis. J Biol Chem. 2005 Nov 18;280(46):38177-85. Epub 2005 Sep 12. PMID:16159874 doi:http://dx.doi.org/10.1074/jbc.M506916200
48. ↑ Gregory LA, Aguissa-Toure AH, Pinaud N, Legrand P, Gleizes PE, Fribourg S. Molecular basis of Diamond-Blackfan anemia: structure and function analysis of RPS19. Nucleic Acids Res. 2007;35(17):5913-21. Epub 2007 Aug 28. PMID:17726054 doi:10.1093/nar/gkm626
49. ↑ Bernstein KA, Gallagher JE, Mitchell BM, Granneman S, Baserga SJ. The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell. 2004 Dec;3(6):1619-26. PMID:15590835 doi:http://dx.doi.org/10.1128/EC.3.6.1619-1626.2004
50. ↑ Ben-Shem A, Garreau de Loubresse N, Melnikov S, Jenner L, Yusupova G, Yusupov M. The structure of the eukaryotic ribosome at 3.0 A resolution. Science. 2011 Dec 16;334(6062):1524-9. Epub 2011 Nov 17. PMID:22096102 doi:10.1126/science.1212642
51. ↑ Presutti C, Ciafre SA, Bozzoni I. The ribosomal protein L2 in S. cerevisiae controls the level of accumulation of its own mRNA. EMBO J. 1991 Aug;10(8):2215-21. PMID:2065661
52. ↑ Tesina P, Heckel E, Cheng J, Fromont-Racine M, Buschauer R, Kater L, Beatrix B, Berninghausen O, Jacquier A, Becker T, Beckmann R. Structure of the 80S ribosome-Xrn1 nuclease complex. Nat Struct Mol Biol. 2019 Mar 25. pii: 10.1038/s41594-019-0202-5. doi:, 10.1038/s41594-019-0202-5. PMID:30911188 doi:http://dx.doi.org/10.1038/s41594-019-0202-5