Ribosomal protein

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010 large subunit-1FFK.gif
A large ribosomal subunit ( PDB: 1FFK ​).
010 small subunit-1FKA.gif
A small ribosomal subunit ( PDB: 1FKA ​).
The two ribosomal subunits. Proteins are shown in blue and the RNA chains in brown and yellow.

A ribosomal protein (r-protein or rProtein [1] [2] [3] ) is any of the proteins that, in conjunction with rRNA, make up the ribosomal subunits involved in the cellular process of translation. E. coli, other bacteria and Archaea have a 30S small subunit and a 50S large subunit, whereas humans and yeasts have a 40S small subunit and a 60S large subunit. [4] Equivalent subunits are frequently numbered differently between bacteria, Archaea, yeasts and humans. [5]

Contents

A large part of the knowledge about these organic molecules has come from the study of E. coli ribosomes. All ribosomal proteins have been isolated and many specific antibodies have been produced. These, together with electronic microscopy and the use of certain reactives, have allowed for the determination of the topography of the proteins in the ribosome. More recently, a near-complete (near)atomic picture of the ribosomal proteins is emerging from the latest high-resolution cryo-EM data (including PDB: 5AFI ​).

Conservation

A 2016 tree of life using 16 universally-conserved ribosomal protein sequences A Novel Representation Of The Tree Of Life.png
A 2016 tree of life using 16 universally-conserved ribosomal protein sequences

Ribosomal proteins are among the most highly conserved proteins across all life forms. [5] Among the 40 proteins found in various small ribosomal subunits (RPSs), 15 subunits are universally conserved across prokaryotes and eukaryotes. However, 7 subunits are only found in bacteria (bS21, bS6, bS16, bS18, bS20, bS21, and bTHX), while 17 subunits are only found in archaea and eukaryotes. [5] Typically 22 proteins are found in bacterial small subunits and 32 in yeast, human and most likely most other eukaryotic species. Twenty-seven (out of 32) proteins of the eukaryotic small ribosomal subunit proteins are also present in archaea (no ribosomal protein is exclusively found in archaea), confirming that they are more closely related to eukaryotes than to bacteria. [5]

Among the large ribosomal subunit (RPLs), 18 proteins are universal, i.e. found in both bacteria, eukaryotes, and archaea. 14 proteins are only found in bacteria, while 27 proteins are only found in archaea and eukaryotes. Again, archaea have no proteins unique to them. [5]

Essentiality

Despite their high conservation over billions of years of evolution, the absence of several ribosomal proteins in certain species shows that ribosomal subunits have been added and lost over the course of evolution. This is also reflected by the fact that several ribosomal proteins do not appear to be essential when deleted. [7] For instance, in E. coli nine ribosomal proteins (uL15, bL21, uL24, bL27, uL29, uL30, bL34, uS9, and uS17) are nonessential for survival when deleted. Taken together with previous results, 22 of the 54 E. coli ribosomal protein genes can be individually deleted from the genome. [8] Similarly, 16 ribosomal proteins (uL1, bL9, uL15, uL22, uL23, bL28, uL29, bL32, bL33.1, bL33.2, bL34, bL35, bL36, bS6, bS20, and bS21) were successfully deleted in Bacillus subtilis . In conjunction with previous reports, 22 ribosomal proteins have been shown to be nonessential in B. subtilis, at least for cell proliferation. [9]

Assembly

In E. coli

The ribosome of E. coli has about 22 proteins in the small subunit (labelled S1 to S22) and 33 proteins in the large subunit (somewhat counter-intuitively called L1 to L36). All of them are different with three exceptions: one protein is found in both subunits (S20 and L26),[ dubious – discuss ] L7 and L12 are acetylated and methylated forms of the same protein, and L8 is a complex of L7/L12 and L10. In addition, L31 is known to exist in two forms, the full length at 7.9 kilodaltons (kDa) and fragmented at 7.0 kDa. This is why the number of proteins in a ribosome is of 56. Except for S1 (with a molecular weight of 61.2 kDa), the other proteins range in weight between 4.4 and 29.7 kDa. [10]

Recent de novo proteomics experiments where the authors characterized in vivo ribosome-assembly intermediates and associated assembly factors from wild-type Escherichia coli cells using a general quantitative mass spectrometry (qMS) approach have confirmed the presence of all the known small and large subunit components and have identified a total of 21 known and potentially new ribosome-assembly-factors that co-localise with various ribosomal particles. [11]

Disposition in the small ribosomal subunit

In the small (30S) subunit of E. coli ribosomes, the proteins denoted uS4, uS7, uS8, uS15, uS17, bS20 bind independently to 16S rRNA. After assembly of these primary binding proteins, uS5, bS6, uS9, uS12, uS13, bS16, bS18, and uS19 bind to the growing ribosome. These proteins also potentiate the addition of uS2, uS3, uS10, uS11, uS14, and bS21. Protein binding to helical junctions is important for initiating the correct tertiary fold of RNA and to organize the overall structure. Nearly all the proteins contain one or more globular domains. Moreover, nearly all contain long extensions that can contact the RNA in far-reaching regions.[ citation needed ] Additional stabilization results from the proteins' basic residues, as these neutralize the charge repulsion of the RNA backbone. Protein–protein interactions also exist to hold structure together by electrostatic and hydrogen bonding interactions. Theoretical investigations pointed to correlated effects of protein-binding onto binding affinities during the assembly process [12]

In one study, the net charges (at pH 7.4) of the ribosomal proteins comprising the highly conserved S10-spc cluster were found to have an inverse relationship with the halophilicity/halotolerance levels in bacteria and archaea. [13] In non-halophilic bacteria, the S10-spc proteins are generally basic, contrasting with the overall acidic whole proteomes of the extremely halophiles. The universal uL2 lying in the oldest part of the ribosome, is always positively charged irrespective of the strain/organism it belongs to. [13]

In eukaryotes

Ribosomes in eukaryotes contain 79–80 proteins and four ribosomal RNA (rRNA) molecules. General or specialized chaperones solubilize the ribosomal proteins and facilitate their import into the nucleus. Assembly of the eukaryotic ribosome appears to be driven by the ribosomal proteins in vivo when assembly is also aided by chaperones. Most ribosomal proteins assemble with rRNA co-transcriptionally, becoming associated more stably as assembly proceeds, and the active sites of both subunits are constructed last. [5]

Table of ribosomal proteins

In the past, different nomenclatures were used for the same ribosomal protein in different organisms. Not only were the names not consistent across domains; the names also differed between organisms within a domain, such as humans and S. cerevisiae , both eukaryotes. This was due to researchers assigning names before the sequences were known, causing trouble for later research. The following tables use the unified nomenclature by Ban et al., 2014. The same nomenclature is used by UniProt's "family" curation. [5]

In general, cellular ribosomal proteins are to be called simply using the cross domain name, e.g. "uL14" for what is currently called L23 in humans. A suffix is used for the organellar versions, so that "uL14m" refers to the human mitochondrial uL14 (MRPL14). [5] Organelle-specific proteins use their own cross-domain prefixes, for example "mS33" for MRPS33 [14] : Table S3, S4  and "cL37" for PSRP5. [15] : Table S2, S3  (See the two proceeding citations, also partially by Ban N, for the organelle nomenclatures.)

Small subunit ribosomal proteins [5]
Cross-domain name [lower-alpha 1] Pfam domainTaxonomic range [lower-alpha 2] Bacteria name (E. coli UniProt)Yeast nameHuman name
bS1 PF00575 BS1 P0AG67 ——
eS1 PF01015 A E—S1 S3A
uS2 PF00318, PF16122 B A ES2 P0A7V0 S0 SA
uS3 PF00189, PF07650 B A ES3 P0A7V3 S3 S3
uS4 PF00163, PF01479 B A ES4 P0A7V8 S9 S9
eS4 PF00900, PF08071, PF16121 A E—S4S4 (X, Y1, Y2)
uS5 PF00333, PF03719 B A ES5 P0A7W1 S2 S2
bS6 PF01250 BS6 P02358 ——
eS6 PF01092 A E—S6 S6
uS7 PF00177 B A ES7 P02359 S5 S5
eS7 PF01251 E—S7 S7
uS8 PF00410 B A ES8 P0A7W7 S22 S15A
eS8 PF01201 A E—S8 S8
uS9 PF00380 B A ES9 P0A7X3 S16 S16
uS10 PF00338 B A ES10 P0A7R5 S20 S20
eS10 PF03501 E—S10 S10
uS11 PF00411 B A ES11 P0A7R9 S14 S14
uS12 PF00164 B A ES12 P0A7S3 S23 S23
eS12 PF01248 E—S12 S12
uS13 PF00416 B A ES13 P0A7S9 S18 S18
uS14 PF00253 B A ES14 P0AG59 S29 S29
uS15 PF00312 B A ES15 P0ADZ4 S13 S13
bS16 PF00886 BS16 P0A7T3 ——
uS17 PF00366 B A ES17 P0AG63 S11 S11
eS17 PF00366 A E—S17 S17
bS18 PF01084 BS18 P0A7T7 ——
uS19 PF00203 B A ES19 P0A7U3 S15 S15
eS19 PF01090 A E—S19 S19
bS20 PF01649 BS20 P0A7U7 ——
bS21 PF01165 BS21 P68681 ——
bTHX PF17070, PF17067 BTHX (missing from E. coli)——
eS21 PF01249 E—S21 S21
eS24 PF01282 A E—S24 S24
eS25 PF03297 A E—S25 S25
eS26 PF01283 E—S26 S26
eS27 PF01667 A E—S27 S27
eS28 PF01200 A E—S28 S28
eS30 PF04758 A E—S30 S30
eS31 PF01599 A E—S31 S27A
RACK1 PF00400 E—Asc1 RACK1
Large subunit ribosomal proteins [5]
Cross-domain name [lower-alpha 1] Pfam domainsTaxonomic range [lower-alpha 2] Bacteria name (E. coli UniProt)Yeast nameHuman name
uL1 PF00687 B A EL1 P0A7L0 L1 L10A
uL2 PF03947, PF00181 B A EL2 P60422 L2 L8
uL3 PF00297 B A EL3 P60438 L3 L3
uL4 PF00573 B A EL4 P60723 L4 L4
uL5 PF00281, PF00673 (b)B A EL5 P62399 L11 L11
uL6 PF00347 B A EL6 P0AG55 L9 L9
eL6 PF01159, PF03868 E—L6 L6
eL8 PF01248 A E—L8 L7A
bL9 PF01281, PF03948 BL9 P0A7R1 ——
uL10 PF00466 B A EL10 P0A7J3 P0 P0
uL11 PF03946, PF00298 B A EL11 P0A7J7 L12 L12
bL12 PF16320, PF00542 BL7/L12 P0A7K2 ——
uL13 PF00572 B A EL13 P0AA10 L16 L13A
eL13 PF01294 A E—L13 L13
uL14 PF00238 B A EL14 P0ADY3 L23 L23
eL14 PF01929 A E—L14 L14
uL15 PF00828 B A EL15 P02413 L28 L27A
eL15 PF00827 A E—L15 L15
uL16 PF00252 B A EL16 P0ADY7 L10 L10
bL17 PF01196 BL17 P0AG44 ——
uL18 PF00861 B A EL18 P0C018 L5 L5
eL18 PF00828 A E—L18 L18
bL19 PF01245 BL19 B1LPB3 ——
eL19 PF01280 A E—L19 L19
bL20 PF00453 BL20 P0A7L3 ——
eL20 PF01775 E—L20 L18A
bL21 PF00829 BL21 P0AG48 ——
eL21 PF01157 A E—L21 L21
uL22 PF00237 B A EL22 P61175 L17 L17
eL22 PF01776 E—L22 L22
uL23 PF00276, PF03939 (e)B A EL23 P0ADZ0 L25 L23A
uL24 PF00467 (b), PF16906 (ae)B A EL24 P60624 L26 L26
eL24 PF01246 A E—L24 L24
bL25 PF01386 BL25 P68919 ——
bL27 PF01016 BL27 P0A7M0 ——
eL27 PF01777 E—L27 L27
bL28 PF00830 BL28 P0A7M2 ——
eL28 PF01778 E—— L28
uL29 PF00831 B A EL29 P0A7M6 L35 L35
eL29 PF01779 E—L29 L29
uL30 PF00327 B A EL30 P0AG51 L7 L7
eL30 PF01248 A E—L30 L30
bL31 PF01197 BL31 P0A7M9 ——
eL31 PF01198 A E—L31 L31
bL32 PF01783 BL32 C4ZS29 ——
eL32 PF01655 A E—L32 L32
bL33 PF00471 BL33 P0A7N9 ——
eL33 PF01247 A E—L33 L35A
bL34 PF00468 BL34 P0A7P6 ——
eL34 PF01199 A E—L34 L34
bL35 PF01632 BL35 P0A7Q2 ——
bL36 PF00444 BL36 P0A7Q7 ——
eL36 PF01158 E—L36 L36
eL37 PF01907 A E—L37 L37
eL38 PF01781 A E—L38 L38
eL39 PF00832 A E—L39 L39
eL40 PF01020 A E—L40 L40
eL41 PF05162 A E—L41 L41
eL42 PF00935 A E—L42 L36A
eL43 PF01780 A E—L43 L37A
P1/P2 PF00428 A E—P1/P2 (AB) P1/P2 (αβ)
  1. 1 2 b = bacteria (+organelle); e = eukarya cytoplasm; u = universal. Older nomenclature often have the order reversed, so that "bS1" becomes S1b or S1p (for "prokaryote").
  2. 1 2 B = bacteria (+organelle); A = archaea; E = eukarya cytoplasm

See also

Related Research Articles

<span class="mw-page-title-main">Ribosome</span> Synthesizes proteins in cells

Ribosomes are macromolecular machines, found within all cells, that perform biological protein synthesis. Ribosomes link amino acids together in the order specified by the codons of messenger RNA molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA molecules and many ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.

<span class="mw-page-title-main">RNA polymerase</span> Enzyme that synthesizes RNA from DNA

In molecular biology, RNA polymerase, or more specifically DNA-directed/dependent RNA polymerase (DdRP), is an enzyme that catalyzes the chemical reactions that synthesize RNA from a DNA template.

<span class="mw-page-title-main">Translation (biology)</span> Cellular process of protein synthesis

In biology, translation is the process in living cells in which proteins are produced using RNA molecules as templates. The generated protein is a sequence of amino acids. This sequence is determined by the sequence of nucleotides in the RNA. The nucleotides are considered three at a time. Each such triple results in addition of one specific amino acid to the protein being generated. The matching from nucleotide triple to amino acid is called the genetic code. The translation is performed by a large complex of functional RNA and proteins called ribosomes. The entire process is called gene expression.

The 5′ untranslated region is the region of a messenger RNA (mRNA) that is directly upstream from the initiation codon. This region is important for the regulation of translation of a transcript by differing mechanisms in viruses, prokaryotes and eukaryotes. While called untranslated, the 5′ UTR or a portion of it is sometimes translated into a protein product. This product can then regulate the translation of the main coding sequence of the mRNA. In many organisms, however, the 5′ UTR is completely untranslated, instead forming a complex secondary structure to regulate translation.

The Shine–Dalgarno (SD) sequence is a ribosomal binding site in bacterial and archaeal messenger RNA, generally located around 8 bases upstream of the start codon AUG. The RNA sequence helps recruit the ribosome to the messenger RNA (mRNA) to initiate protein synthesis by aligning the ribosome with the start codon. Once recruited, tRNA may add amino acids in sequence as dictated by the codons, moving downstream from the translational start site.

<span class="mw-page-title-main">Ribosomal RNA</span> RNA component of the ribosome, essential for protein synthesis in all living organisms

Ribosomal ribonucleic acid (rRNA) is a type of non-coding RNA which is the primary component of ribosomes, essential to all cells. rRNA is a ribozyme which carries out protein synthesis in ribosomes. Ribosomal RNA is transcribed from ribosomal DNA (rDNA) and then bound to ribosomal proteins to form small and large ribosome subunits. rRNA is the physical and mechanical factor of the ribosome that forces transfer RNA (tRNA) and messenger RNA (mRNA) to process and translate the latter into proteins. Ribosomal RNA is the predominant form of RNA found in most cells; it makes up about 80% of cellular RNA despite never being translated into proteins itself. Ribosomes are composed of approximately 60% rRNA and 40% ribosomal proteins, though this ratio differs between prokaryotes and eukaryotes.

<span class="mw-page-title-main">Start codon</span> First codon of a messenger RNA translated by a ribosome

The start codon is the first codon of a messenger RNA (mRNA) transcript translated by a ribosome. The start codon always codes for methionine in eukaryotes and archaea and a N-formylmethionine (fMet) in bacteria, mitochondria and plastids.

Bacterial translation is the process by which messenger RNA is translated into proteins in bacteria.

Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recapping.

Elongation factor 4 (EF-4) is an elongation factor that is thought to back-translocate on the ribosome during the translation of RNA to proteins. It is found near-universally in bacteria and in eukaryotic endosymbiotic organelles including the mitochondria and the plastid. Responsible for proofreading during protein synthesis, EF-4 is a recent addition to the nomenclature of bacterial elongation factors.

<span class="mw-page-title-main">5S ribosomal RNA</span> RNA component of the large subunit of the ribosome

The 5S ribosomal RNA is an approximately 120 nucleotide-long ribosomal RNA molecule with a mass of 40 kDa. It is a structural and functional component of the large subunit of the ribosome in all domains of life, with the exception of mitochondrial ribosomes of fungi and animals. The designation 5S refers to the molecule's sedimentation coefficient in an ultracentrifuge, which is measured in Svedberg units (S).

A ribosome binding site, or ribosomal binding site (RBS), is a sequence of nucleotides upstream of the start codon of an mRNA transcript that is responsible for the recruitment of a ribosome during the initiation of translation. Mostly, RBS refers to bacterial sequences, although internal ribosome entry sites (IRES) have been described in mRNAs of eukaryotic cells or viruses that infect eukaryotes. Ribosome recruitment in eukaryotes is generally mediated by the 5' cap present on eukaryotic mRNAs.

<span class="mw-page-title-main">Signal recognition particle RNA</span>

The signal recognition particle RNA, is part of the signal recognition particle (SRP) ribonucleoprotein complex. SRP recognizes the signal peptide and binds to the ribosome, halting protein synthesis. SRP-receptor is a protein that is embedded in a membrane, and which contains a transmembrane pore. When the SRP-ribosome complex binds to SRP-receptor, SRP releases the ribosome and drifts away. The ribosome resumes protein synthesis, but now the protein is moving through the SRP-receptor transmembrane pore.

<span class="mw-page-title-main">Prokaryotic large ribosomal subunit</span>

50S is the larger subunit of the 70S ribosome of prokaryotes, i.e. bacteria and archaea. It is the site of inhibition for antibiotics such as macrolides, chloramphenicol, clindamycin, and the pleuromutilins. It includes the 5S ribosomal RNA and 23S ribosomal RNA.

Ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. The 60S subunit is the large subunit of eukaryotic 80S ribosomes, with the other major component being the eukaryotic small ribosomal subunit (40S). It is structurally and functionally related to the 50S subunit of 70S prokaryotic ribosomes. However, the 60S subunit is much larger than the prokaryotic 50S subunit and contains many additional protein segments, as well as ribosomal RNA expansion segments.

<span class="mw-page-title-main">40S ribosomal protein S5</span> Protein-coding gene in the species Homo sapiens

40S ribosomal protein S5 is a ribosomal subunit of the Eukaryotic ribosome (80S) complex. In humans it is encoded by the RPS5 gene.

The eukaryotic small ribosomal subunit (40S) is the smaller subunit of the eukaryotic 80S ribosomes, with the other major component being the large ribosomal subunit (60S). The "40S" and "60S" names originate from the convention that ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. It is structurally and functionally related to the 30S subunit of 70S prokaryotic ribosomes. However, the 40S subunit is much larger than the prokaryotic 30S subunit and contains many additional protein segments, as well as rRNA expansion segments.

<span class="mw-page-title-main">Eukaryotic ribosome</span> Large and complex molecular machine

Ribosomes are a large and complex molecular machine that catalyzes the synthesis of proteins, referred to as translation. The ribosome selects aminoacylated transfer RNAs (tRNAs) based on the sequence of a protein-encoding messenger RNA (mRNA) and covalently links the amino acids into a polypeptide chain. Ribosomes from all organisms share a highly conserved catalytic center. However, the ribosomes of eukaryotes are much larger than prokaryotic ribosomes and subject to more complex regulation and biogenesis pathways. Eukaryotic ribosomes are also known as 80S ribosomes, referring to their sedimentation coefficients in Svedberg units, because they sediment faster than the prokaryotic (70S) ribosomes. Eukaryotic ribosomes have two unequal subunits, designated small subunit (40S) and large subunit (60S) according to their sedimentation coefficients. Both subunits contain dozens of ribosomal proteins arranged on a scaffold composed of ribosomal RNA (rRNA). The small subunit monitors the complementarity between tRNA anticodon and mRNA, while the large subunit catalyzes peptide bond formation.

<span class="mw-page-title-main">Mitochondrial ribosome</span> Protein complex

The mitochondrial ribosome, or mitoribosome, is a protein complex that is active in mitochondria and functions as a riboprotein for translating mitochondrial mRNAs encoded in mtDNA. The mitoribosome is attached to the inner mitochondrial membrane. Mitoribosomes, like cytoplasmic ribosomes, consist of two subunits — large (mt-LSU) and small (mt-SSU). Mitoribosomes consist of several specific proteins and fewer rRNAs. While mitochondrial rRNAs are encoded in the mitochondrial genome, the proteins that make up mitoribosomes are encoded in the nucleus and assembled by cytoplasmic ribosomes before being implanted into the mitochondria.

Archaeal initiation factors are proteins that are used during the translation step of protein synthesis in archaea. The principal functions these proteins perform include ribosome RNA/mRNA recognition, delivery of the initiator Met-tRNAiMet, methionine bound tRNAi, to the 40s ribosome, and proofreading of the initiation complex.

References

  1. ↑ Salini Konikkat: Dynamic Remodeling Events Drive the Removal of the ITS2 Spacer Sequence During Assembly of 60S Ribosomal Subunits in S. cerevisiae. Carnegie Mellon University Dissertations, Feb. 2016.
  2. ↑ Weiler EW, Nover L (2008). Allgemeine und molekulare Botanik (in German). Stuttgart: Georg Thieme Verlag. p. 532. ISBN   978-3-13-152791-2.
  3. ↑ de la Cruz J, Karbstein K, Woolford JL (2015). "Functions of ribosomal proteins in assembly of eukaryotic ribosomes in vivo". Annual Review of Biochemistry (in German). 84: 93–129. doi:10.1146/annurev-biochem-060614-033917. PMC   4772166 . PMID   25706898.
  4. ↑ Rodnina MV, Wintermeyer W (April 2011). "The ribosome as a molecular machine: the mechanism of tRNA-mRNA movement in translocation". Biochemical Society Transactions. 39 (2): 658–62. doi:10.1042/BST0390658. PMID   21428957.
  5. 1 2 3 4 5 6 7 8 9 10 Ban N, Beckmann R, Cate JH, Dinman JD, Dragon F, Ellis SR, et al. (February 2014). "A new system for naming ribosomal proteins". Current Opinion in Structural Biology. 24: 165–9. doi:10.1016/j.sbi.2014.01.002. PMC   4358319 . PMID   24524803.
  6. ↑ Hug LA, Baker BJ, Anantharaman K, Brown CT, Probst AJ, Castelle CJ, et al. (April 2016). "A new view of the tree of life". Nature Microbiology. 1 (5): 16048. doi: 10.1038/nmicrobiol.2016.48 . PMID   27572647.
  7. ↑ Gao F, Luo H, Zhang CT, Zhang R (2015). "Gene Essentiality Analysis Based on DEG 10, an Updated Database of Essential Genes". Gene Essentiality. Methods in Molecular Biology. Vol. 1279. pp. 219–33. doi:10.1007/978-1-4939-2398-4_14. ISBN   978-1-4939-2397-7. PMID   25636622.
  8. ↑ Shoji S, Dambacher CM, Shajani Z, Williamson JR, Schultz PG (November 2011). "Systematic chromosomal deletion of bacterial ribosomal protein genes". Journal of Molecular Biology. 413 (4): 751–61. doi:10.1016/j.jmb.2011.09.004. PMC   3694390 . PMID   21945294.
  9. ↑ Akanuma G, Nanamiya H, Natori Y, Yano K, Suzuki S, Omata S, et al. (November 2012). "Inactivation of ribosomal protein genes in Bacillus subtilis reveals importance of each ribosomal protein for cell proliferation and cell differentiation". Journal of Bacteriology. 194 (22): 6282–91. doi:10.1128/JB.01544-12. PMC   3486396 . PMID   23002217.
  10. ↑ Arnold RJ, Reilly JP (April 1999). "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry". Analytical Biochemistry. 269 (1): 105–12. doi:10.1006/abio.1998.3077. PMID   10094780.
  11. ↑ Chen SS, Williamson JR (February 2013). "Characterization of the ribosome biogenesis landscape in E. coli using quantitative mass spectrometry". Journal of Molecular Biology. 425 (4): 767–79. doi:10.1016/j.jmb.2012.11.040. PMC   3568210 . PMID   23228329.
  12. ↑ Hamacher K, Trylska J, McCammon JA (February 2006). "Dependency map of proteins in the small ribosomal subunit". PLOS Computational Biology. 2 (2): e10. Bibcode:2006PLSCB...2...10H. doi: 10.1371/journal.pcbi.0020010 . PMC   1364506 . PMID   16485038.
  13. 1 2 Tirumalai MR, Anane-Bediakoh D, Rajesh R, Fox GE (November 2021). "Net Charges of the Ribosomal Proteins of the S10 and spc Clusters of Halophiles Are Inversely Related to the Degree of Halotolerance". Microbiol. Spectr. 9 (3): e0178221. doi:10.1128/spectrum.01782-21. PMC   8672879 . PMID   34908470.
  14. ↑ Greber BJ, Bieri P, Leibundgut M, Leitner A, Aebersold R, Boehringer D, Ban N (April 2015). "Ribosome. The complete structure of the 55S mammalian mitochondrial ribosome". Science. 348 (6232): 303–8. doi:10.1126/science.aaa3872. hdl: 20.500.11850/100390 . PMID   25837512. S2CID   206634178.
  15. ↑ Bieri, P; Leibundgut, M; Saurer, M; Boehringer, D; Ban, N (15 February 2017). "The complete structure of the chloroplast 70S ribosome in complex with translation factor pY". The EMBO Journal. 36 (4): 475–486. doi:10.15252/embj.201695959. PMC   5694952 . PMID   28007896.

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