Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function

The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structur...

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Published inInternational journal of molecular sciences Vol. 24; no. 4; p. 3386
Main Authors Qiu, Lijuan, Chao, Wen, Zhong, Shan, Ren, An-Jing
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 08.02.2023
MDPI
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ISSN1422-0067
1661-6596
1422-0067
DOI10.3390/ijms24043386

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Abstract The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed.
AbstractList The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed.
The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed.The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed.
Audience Academic
Author Qiu, Lijuan
Ren, An-Jing
Zhong, Shan
Chao, Wen
AuthorAffiliation Experimental Teaching Center, College of Basic Medical Sciences, Naval Medical University, Shanghai 200433, China
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Cites_doi 10.1002/cbic.201300318
10.1146/annurev-biochem-060713-035445
10.1146/annurev-pathol-011110-130246
10.1093/nar/29.3.677
10.1016/S0021-9258(17)32308-6
10.1017/S1355838299991550
10.32607/20758251-2012-4-4-65-72
10.1016/j.jmb.2009.07.049
10.1016/j.cell.2019.10.035
10.7554/eLife.07939
10.1093/jxb/erw106
10.1074/jbc.M306534200
10.1371/journal.pone.0032552
10.1261/rna.688207
10.1016/S0021-9258(19)74040-X
10.1006/jsbi.1997.3907
10.1016/j.bbrc.2019.03.166
10.1074/jbc.M102416200
10.1002/jcb.21722
10.1177/17085381211026474
10.1155/2022/9943571
10.7554/eLife.22572
10.1093/nar/gkp1113
10.1046/j.1432-1327.1999.00901.x
10.4161/rna.29545
10.1126/science.1060089
10.1038/sj.emboj.7600102
10.1016/j.neulet.2021.136389
10.3892/ijo.2015.3017
10.1126/science.1198308
10.1006/jmbi.1998.1780
10.1038/s41586-021-04131-9
10.1093/nar/gkt632
10.32607/actanaturae.11540
10.1371/journal.pone.0203415
10.1016/j.tibs.2017.03.004
10.1134/S0026893309040177
10.1016/S0092-8674(01)00539-6
10.1016/j.micinf.2019.06.008
10.1016/S0969-2126(97)00270-0
10.1093/nar/gkv110
10.15252/embj.2022110581
10.3390/ijms20133290
10.1074/jbc.272.23.14547
10.1016/j.vetmic.2020.108858
10.1017/S1355838200001199
10.1042/bj2080289
10.1016/S1046-5928(02)00652-6
10.1002/j.1460-2075.1995.tb00137.x
10.1093/genetics/iyab176
10.1002/hep.27138
10.3389/fmolb.2021.654164
10.1042/BST20160106
10.1016/j.febslet.2004.11.026
10.1016/j.biochi.2018.02.016
10.1016/S0022-2836(05)80020-8
10.1016/j.exppara.2020.107870
10.1016/j.biochi.2009.06.013
10.1093/oxfordjournals.jbchem.a003036
10.1038/ncomms8646
10.1007/BF00268450
10.1006/jmbi.2000.3563
10.1007/0-306-48158-8_6
10.1016/0167-4781(95)00045-I
10.1371/journal.pone.0010194
10.1016/j.cell.2004.08.001
10.1098/rstb.2016.0177
10.1101/gad.1397906
10.1242/dev.128.21.4289
10.1038/s41598-018-19652-z
10.1073/pnas.1620569114
10.1016/j.dci.2021.104212
10.1093/nar/gku550
10.1016/j.sbi.2012.07.013
10.1126/science.1212642
10.1093/nar/23.22.4616
10.1021/acs.chemrev.9b00742
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Issue 4
Keywords translation
cancer
ribosomal protein S5
liver disease
function
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References Robert (ref_49) 2000; 6
Kuwano (ref_7) 1993; 267
Friedman (ref_69) 2011; 6
ref_14
Greuer (ref_38) 1999; 5
Quade (ref_62) 2015; 6
Miyamoto (ref_28) 1999; 266
Matragkou (ref_18) 2008; 104
Bhat (ref_59) 2015; 43
Pan (ref_73) 2022; 2022
Urlaub (ref_47) 1995; 14
Francis (ref_76) 1982; 208
Saito (ref_39) 1994; 235
Fredrick (ref_36) 2000; 298
Wang (ref_5) 2021; 125
Visweswaraiah (ref_57) 2015; 4
Davies (ref_23) 1998; 279
Sharifulin (ref_51) 2013; 14
Stainslas (ref_58) 2019; 21
Pelava (ref_10) 2016; 44
Galkin (ref_13) 2007; 13
Joseph (ref_65) 2014; 11
Bischof (ref_44) 1994; 269
Paez (ref_70) 2004; 115
Johnson (ref_64) 2017; 372
Hosaka (ref_26) 2001; 130
Matragkou (ref_56) 2009; 392
Robert (ref_34) 2001; 29
Djumagulov (ref_29) 2021; 600
Hosaka (ref_45) 1997; 5
Tomioka (ref_68) 2018; 8
Spahn (ref_52) 2004; 118
Dong (ref_66) 2017; 114
Ignatovich (ref_9) 1995; 23
Bheemireddy (ref_33) 2021; 8
Guo (ref_67) 2020; 249
Harada (ref_25) 1997; 120
Su (ref_72) 2021; 30
ref_32
Noller (ref_37) 2005; 579
Hinnebusch (ref_53) 2017; 42
Weijers (ref_74) 2001; 128
Moraleva (ref_2) 2022; 14
Malygin (ref_42) 2009; 91
Babaylova (ref_61) 2018; 148
Garreau (ref_4) 2011; 334
Yang (ref_21) 2022; 769
Malygin (ref_24) 2003; 28
Malygin (ref_41) 2009; 43
Zhang (ref_75) 2016; 67
Jenner (ref_3) 2012; 22
Vizirianakis (ref_71) 1999; 11
Rabl (ref_30) 2011; 331
Golovin (ref_46) 2012; 4
Vizirianakis (ref_19) 2015; 47
Tsukihashi (ref_55) 2001; 276
Yusupov (ref_11) 2001; 292
Visweswaraiah (ref_16) 2017; 6
Pisarev (ref_54) 2006; 20
Dong (ref_17) 2022; 220
Malygin (ref_63) 2013; 41
Duss (ref_35) 2019; 179
Robert (ref_40) 2003; 278
Li (ref_27) 2019; 512
ref_43
Xu (ref_20) 2014; 60
Yusupova (ref_31) 2014; 83
Madjar (ref_77) 1980; 179
Spahn (ref_12) 2004; 23
Bowman (ref_1) 2020; 120
Ghosh (ref_15) 2014; 42
Urlaub (ref_48) 1997; 272
Spahn (ref_50) 2001; 107
Brown (ref_60) 2022; 41
Lumsden (ref_22) 2010; 38
Frigerio (ref_8) 1995; 1262
Tian (ref_78) 2020; 212
ref_6
References_xml – volume: 14
  start-page: 2136
  year: 2013
  ident: ref_51
  article-title: Ribosomal protein S5e is implicated in translation initiation through its interaction with the N-terminal domain of initiation factor eIF2α
  publication-title: Chembiochem
  doi: 10.1002/cbic.201300318
– volume: 83
  start-page: 467
  year: 2014
  ident: ref_31
  article-title: High-resolution structure of the eukaryotic 80S ribosome
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev-biochem-060713-035445
– volume: 6
  start-page: 425
  year: 2011
  ident: ref_69
  article-title: Pathogenesis of liver fibrosis
  publication-title: Annu. Rev. Pathol.-Mech.
  doi: 10.1146/annurev-pathol-011110-130246
– volume: 29
  start-page: 677
  year: 2001
  ident: ref_34
  article-title: Ribosomal protein S7 from Escherichia coli uses the same determinants to bind 16S ribosomal RNA and its messenger RNA
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/29.3.677
– volume: 269
  start-page: 18315
  year: 1994
  ident: ref_44
  article-title: Analysis of the puromycin binding site in the 70 S ribosome of Escherichia coli at the peptide level
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)32308-6
– volume: 5
  start-page: 1521
  year: 1999
  ident: ref_38
  article-title: The cross-link from the upstream region of mRNA to ribosomal protein S7 is located in the C-terminal peptide: Experimental verification of a prediction from modeling studies
  publication-title: RNA
  doi: 10.1017/S1355838299991550
– volume: 4
  start-page: 65
  year: 2012
  ident: ref_46
  article-title: Identification of Novel RNA-Protein Contact in Complex of Ribosomal Protein S7 and 3′-Terminal Fragment of 16S rRNA in E. coli
  publication-title: Acta Nat.
  doi: 10.32607/20758251-2012-4-4-65-72
– volume: 392
  start-page: 1192
  year: 2009
  ident: ref_56
  article-title: On the intracellular trafficking of mouse S5 ribosomal protein from cytoplasm to nucleoli
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.07.049
– volume: 179
  start-page: 1357
  year: 2019
  ident: ref_35
  article-title: Transient Protein-RNA Interactions Guide Nascent Ribosomal RNA Folding
  publication-title: Cell
  doi: 10.1016/j.cell.2019.10.035
– volume: 11
  start-page: 409
  year: 1999
  ident: ref_71
  article-title: Expression of ribosomal protein S5 cloned gene during differentiation and apoptosis in murine erythroleukemia (MEL) cells
  publication-title: Oncol. Res.
– volume: 4
  start-page: e7939
  year: 2015
  ident: ref_57
  article-title: The β -hairpin of 40S exit channel protein Rps5/uS7 promotes efficient and accurate translation initiation in vivo
  publication-title: eLife
  doi: 10.7554/eLife.07939
– volume: 67
  start-page: 2731
  year: 2016
  ident: ref_75
  article-title: Plastid ribosomal protein S5 is involved in photosynthesis, plant development, and cold stress tolerance in Arabidopsis
  publication-title: J. Exp. Bot.
  doi: 10.1093/jxb/erw106
– volume: 278
  start-page: 44913
  year: 2003
  ident: ref_40
  article-title: A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M306534200
– ident: ref_14
  doi: 10.1371/journal.pone.0032552
– volume: 13
  start-page: 2116
  year: 2007
  ident: ref_13
  article-title: Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5
  publication-title: RNA
  doi: 10.1261/rna.688207
– volume: 267
  start-page: 25304
  year: 1993
  ident: ref_7
  article-title: The primary structure of rat ribosomal protein S5. A ribosomal protein present in the rat genome in a single copy
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)74040-X
– volume: 120
  start-page: 112
  year: 1997
  ident: ref_25
  article-title: Crystallization and preliminary X-ray crystallographic study of the ribosomal protein S7 from Bacillus stearothermophilus
  publication-title: J. Struct. Biol.
  doi: 10.1006/jsbi.1997.3907
– volume: 512
  start-page: 838
  year: 2019
  ident: ref_27
  article-title: Structural insights into the complex of trigger factor chaperone and ribosomal protein S7 from Mycobacterium tuberculosis
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2019.03.166
– volume: 276
  start-page: 25715
  year: 2001
  ident: ref_55
  article-title: Requirement for yeast TAF145 function in transcriptional activation of the RPS5 promoter that depends on both core promoter structure and upstream activating sequences
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M102416200
– volume: 104
  start-page: 1477
  year: 2008
  ident: ref_18
  article-title: The potential role of ribosomal protein S5 on cell cycle arrest and initiation of murine erythroleukemia cell differentiation
  publication-title: J. Cell. Biochem.
  doi: 10.1002/jcb.21722
– volume: 30
  start-page: 639
  year: 2021
  ident: ref_72
  article-title: Identification of key genes and pathways involved in abdominal aortic aneurysm initiation and progression
  publication-title: Vascular
  doi: 10.1177/17085381211026474
– volume: 2022
  start-page: 9943571
  year: 2022
  ident: ref_73
  article-title: Identification of Key Genes and Pathways Involved in Circulating Tumor Cells in Colorectal Cancer
  publication-title: Anal. Cell. Pathol.
  doi: 10.1155/2022/9943571
– volume: 6
  start-page: e22572
  year: 2017
  ident: ref_16
  article-title: Interface between 40S exit channel protein uS7/Rps5 and eIF2α modulates start codon recognition in vivo
  publication-title: eLife
  doi: 10.7554/eLife.22572
– volume: 38
  start-page: 1261
  year: 2010
  ident: ref_22
  article-title: Yeast strains with N-terminally truncated ribosomal protein S5: Implications for the evolution, structure and function of the Rps5/Rps7 proteins
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkp1113
– volume: 266
  start-page: 591
  year: 1999
  ident: ref_28
  article-title: Role of the N-terminal region of ribosomal protein S7 in its interaction with 16S rRNA which binds to the concavity formed by the beta-ribbon arm and the alpha-helix
  publication-title: Eur. J. Biochem.
  doi: 10.1046/j.1432-1327.1999.00901.x
– volume: 11
  start-page: 891
  year: 2014
  ident: ref_65
  article-title: Re-analysis of cryoEM data on HCV IRES bound to 40S subunit of human ribosome integrated with recent structural information suggests new contact regions between ribosomal proteins and HCV RNA
  publication-title: RNA Biol.
  doi: 10.4161/rna.29545
– volume: 292
  start-page: 883
  year: 2001
  ident: ref_11
  article-title: Crystal structure of the ribosome at 5.5 A resolution
  publication-title: Science
  doi: 10.1126/science.1060089
– volume: 23
  start-page: 1008
  year: 2004
  ident: ref_12
  article-title: Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7600102
– volume: 769
  start-page: 136389
  year: 2022
  ident: ref_21
  article-title: Exosomes from hypoxic pre-treated ADSCs attenuateacute ischemic stroke-induced brain injury via delivery of circ-Rps5 and promote M2 microglia/macrophage polarization
  publication-title: Neurosci. Lett.
  doi: 10.1016/j.neulet.2021.136389
– volume: 47
  start-page: 303
  year: 2015
  ident: ref_19
  article-title: Genetic manipulation of RPS5 gene expression modulates the initiation of commitment of MEL cells to erythroid maturation: Implications in understanding ribosomopathies
  publication-title: Int. J. Oncol.
  doi: 10.3892/ijo.2015.3017
– volume: 331
  start-page: 730
  year: 2011
  ident: ref_30
  article-title: Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
  publication-title: Science
  doi: 10.1126/science.1198308
– volume: 279
  start-page: 873
  year: 1998
  ident: ref_23
  article-title: Ribosomal proteins S5 and L6: High-resolution crystal structures and roles in protein synthesis and antibiotic resistance
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1998.1780
– volume: 600
  start-page: 543
  year: 2021
  ident: ref_29
  article-title: Accuracy mechanism of eukaryotic ribosome translocation
  publication-title: Nature
  doi: 10.1038/s41586-021-04131-9
– volume: 41
  start-page: 8706
  year: 2013
  ident: ref_63
  article-title: HCV IRES interacts with the 18S rRNA to activate the 40S ribosome for subsequent steps of translation initiation
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkt632
– volume: 14
  start-page: 14
  year: 2022
  ident: ref_2
  article-title: Eukaryotic Ribosome Biogenesis: The 40S Subunit
  publication-title: Acta Nat.
  doi: 10.32607/actanaturae.11540
– ident: ref_6
  doi: 10.1371/journal.pone.0203415
– volume: 42
  start-page: 589
  year: 2017
  ident: ref_53
  article-title: Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2017.03.004
– volume: 43
  start-page: 643
  year: 2009
  ident: ref_41
  article-title: The mutual effect of human ribosomal proteins S5 and S16 on their binding with 18S rRNA fragment 1203–1236/1521–1698
  publication-title: Mol. Biol.
  doi: 10.1134/S0026893309040177
– volume: 107
  start-page: 373
  year: 2001
  ident: ref_50
  article-title: Structure of the 80S ribosome from Saccharomyces cerevisiae—tRNA-ribosome and subunit-subunit interactions
  publication-title: Cell
  doi: 10.1016/S0092-8674(01)00539-6
– volume: 21
  start-page: 263
  year: 2019
  ident: ref_58
  article-title: The remarkable history of the hepatitis C virus
  publication-title: Microbes Infect.
  doi: 10.1016/j.micinf.2019.06.008
– volume: 5
  start-page: 1199
  year: 1997
  ident: ref_45
  article-title: Ribosomal protein S7: A new RNA-binding motif with structural similarities to a DNA architectural factor
  publication-title: Structure
  doi: 10.1016/S0969-2126(97)00270-0
– volume: 43
  start-page: 2888
  year: 2015
  ident: ref_59
  article-title: The beta hairpin structure within ribosomal protein S5 mediates interplay between domains II and IV and regulates HCV IRES function
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkv110
– volume: 41
  start-page: e110581
  year: 2022
  ident: ref_60
  article-title: Molecular architecture of 40S translation initiation complexes on IRES
  publication-title: EMBO J.
  doi: 10.15252/embj.2022110581
– ident: ref_43
  doi: 10.3390/ijms20133290
– volume: 272
  start-page: 14547
  year: 1997
  ident: ref_48
  article-title: Identification and sequence analysis of contact sites between ribosomal proteins and rRNA in Escherichia coli 30 S subunits by a new approach using matrix-assisted laser desorption/ionization-mass spectrometry combined with N-terminal microsequencing
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.23.14547
– volume: 249
  start-page: 108858
  year: 2020
  ident: ref_67
  article-title: RPS5 interacts with the rabbit hemorrhagic disease virus 3′ extremities region and plays a role in virus replication
  publication-title: Vet. Microbiol.
  doi: 10.1016/j.vetmic.2020.108858
– volume: 6
  start-page: 1649
  year: 2000
  ident: ref_49
  article-title: Mapping of the RNA recognition site of Escherichia coli ribosomal protein S7
  publication-title: RNA
  doi: 10.1017/S1355838200001199
– volume: 208
  start-page: 289
  year: 1982
  ident: ref_76
  article-title: Influence of the state of ribosome association on the phosphorylation of ribosomal proteins in isolated ribosome--protein kinase systems from rat cerebral cortex
  publication-title: Biochem. J.
  doi: 10.1042/bj2080289
– volume: 28
  start-page: 57
  year: 2003
  ident: ref_24
  article-title: Expression and purification of human ribosomal proteins S3, S5, S10, S19, and S26
  publication-title: Protein Expr. Purif.
  doi: 10.1016/S1046-5928(02)00652-6
– volume: 14
  start-page: 4578
  year: 1995
  ident: ref_47
  article-title: Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1995.tb00137.x
– volume: 220
  start-page: iyab176
  year: 2022
  ident: ref_17
  article-title: uS5/Rps2 residues at the 40S ribosome entry channel enhance initiation at suboptimal start codons in vivo
  publication-title: Genetics
  doi: 10.1093/genetics/iyab176
– volume: 60
  start-page: 648
  year: 2014
  ident: ref_20
  article-title: Bioactive compound reveals a novel function for ribosomal protein S5 in hepatic stellate cell activation and hepatic fibrosis
  publication-title: Hepatology
  doi: 10.1002/hep.27138
– volume: 8
  start-page: 654164
  year: 2021
  ident: ref_33
  article-title: Comparative Analysis of Structural and Dynamical Features of Ribosome Upon Association With mRNA Reveals Potential Role of Ribosomal Proteins
  publication-title: Front. Mol. Biosci.
  doi: 10.3389/fmolb.2021.654164
– volume: 44
  start-page: 1086
  year: 2016
  ident: ref_10
  article-title: The importance of ribosome production, and the 5S RNP–MDM2 pathway, in health and disease
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST20160106
– volume: 579
  start-page: 855
  year: 2005
  ident: ref_37
  article-title: The 30S ribosomal P site: A function of 16S rRNA
  publication-title: FEBS Lett.
  doi: 10.1016/j.febslet.2004.11.026
– volume: 148
  start-page: 72
  year: 2018
  ident: ref_61
  article-title: Arrangements ofnucleotides flanking the start codon in the IRES of the hepatitis C virus in the IRES binary complex with the human 40S ribosomal subunit
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2018.02.016
– volume: 235
  start-page: 111
  year: 1994
  ident: ref_39
  article-title: Post-transcriptional regulation of the str operon in Escherichia coli. Ribosomal protein S7 inhibits coupled translation of S7 but not its independent translation
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(05)80020-8
– volume: 212
  start-page: 107870
  year: 2020
  ident: ref_78
  article-title: Comparative evaluation of two informative markers in the phylogeny of Babesia and Theileria parasites
  publication-title: Exp. Parasitol.
  doi: 10.1016/j.exppara.2020.107870
– volume: 91
  start-page: 1180
  year: 2009
  ident: ref_42
  article-title: Interactions of human ribosomal proteins S16 and S5 with an 18S rRNA fragment containing their binding sites
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2009.06.013
– volume: 130
  start-page: 695
  year: 2001
  ident: ref_26
  article-title: The structure of the archaebacterial ribosomal protein S7 and its possible interaction with 16S rRNA
  publication-title: J. Biochem.
  doi: 10.1093/oxfordjournals.jbchem.a003036
– volume: 6
  start-page: 7646
  year: 2015
  ident: ref_62
  article-title: Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms8646
– volume: 179
  start-page: 89
  year: 1980
  ident: ref_77
  article-title: Differences in electrophoretic behaviour of eight ribosomal proteins from rat and rabbit tissues and evidence for proteolytic action on liver proteins
  publication-title: Mol. Gen. Genet.
  doi: 10.1007/BF00268450
– volume: 298
  start-page: 379
  year: 2000
  ident: ref_36
  article-title: Tagging ribosomal protein S7 allows rapid identification of mutants defective in assembly and function of 30 S subunits
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2000.3563
– volume: 115
  start-page: 145
  year: 2004
  ident: ref_70
  article-title: PI3K/PTEN/AKT pathway: A critical mediator of oncogenic signaling
  publication-title: Cancer Treat Res.
  doi: 10.1007/0-306-48158-8_6
– volume: 1262
  start-page: 64
  year: 1995
  ident: ref_8
  article-title: Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0167-4781(95)00045-I
– ident: ref_32
  doi: 10.1371/journal.pone.0010194
– volume: 118
  start-page: 465
  year: 2004
  ident: ref_52
  article-title: Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: The IRES functions as an RNA-based translation factor
  publication-title: Cell
  doi: 10.1016/j.cell.2004.08.001
– volume: 372
  start-page: 20160177
  year: 2017
  ident: ref_64
  article-title: Dynamics of IRES-mediated translation
  publication-title: Philos. Trans. R. Soc. B
  doi: 10.1098/rstb.2016.0177
– volume: 20
  start-page: 624
  year: 2006
  ident: ref_54
  article-title: Specific functional interactions of nucleotides at key −3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
  publication-title: Gene Dev.
  doi: 10.1101/gad.1397906
– volume: 128
  start-page: 4289
  year: 2001
  ident: ref_74
  article-title: An Arabidopsis Minute-like phenotype caused by a semi-dominant mutation in a RIBOSOMAL PROTEIN S5 gene
  publication-title: Development
  doi: 10.1242/dev.128.21.4289
– volume: 8
  start-page: 1244
  year: 2018
  ident: ref_68
  article-title: Ribosomal protein uS7/Rps5 serine-223 in protein kinase-mediated phosphorylation and ribosomal small subunit maturation
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-018-19652-z
– volume: 114
  start-page: E2126
  year: 2017
  ident: ref_66
  article-title: Rps3/uS3 promotes mRNA binding at the 40S ribosome entry channel and stabilizes preinitiation complexes at start codons
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1620569114
– volume: 125
  start-page: 104212
  year: 2021
  ident: ref_5
  article-title: 40S ribosomal protein S18 is a novel maternal peptidoglycan-binding protein that protects embryos of zebrafish from bacterial infections
  publication-title: Dev. Comp. Immunol.
  doi: 10.1016/j.dci.2021.104212
– volume: 42
  start-page: 8537
  year: 2014
  ident: ref_15
  article-title: Rps5-Rps16 communication is essential for efficient translation initiation in yeast S. cerevisiae
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gku550
– volume: 22
  start-page: 759
  year: 2012
  ident: ref_3
  article-title: Crystal structure of the 80S yeast ribosome
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2012.07.013
– volume: 334
  start-page: 1524
  year: 2011
  ident: ref_4
  article-title: The structure of the eukaryotic ribosome at 3.0 Å resolution
  publication-title: Science
  doi: 10.1126/science.1212642
– volume: 23
  start-page: 4616
  year: 1995
  ident: ref_9
  article-title: Cloning and characterisation of the gene encoding the ribosomal protein S5 (also known as rp14, S2, YS8) of Saccharomyces cerevisiae
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/23.22.4616
– volume: 120
  start-page: 4848
  year: 2020
  ident: ref_1
  article-title: Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
  publication-title: Chem. Rev.
  doi: 10.1021/acs.chemrev.9b00742
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Snippet The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role...
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SubjectTerms Amino acids
Apoptosis
Cell division
Eukaryota - genetics
Genetic translation
Humans
Insects
Liver diseases
Mutation
Prokaryotes
Protein synthesis
Proteins
Review
Ribosomal Proteins - metabolism
Ribosomes - metabolism
RNA
RNA, Ribosomal, 18S - metabolism
Transfer RNA
Yeast
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Title Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
URI https://www.ncbi.nlm.nih.gov/pubmed/36834797
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Volume 24
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