Ribosomes:

Introduction:
They are also called structural RNAs for they act as structural components of Ribosome organelle.  The ribosome in its entirety is constructed on ribosomal RNA as a scaffold on which riboproteins are sequentially built to produce a highly dynamic structure, which has astounding abilities to function as translation machine. 

An excellent over view of ribosomal subunits hugging to each other.

Distribution:

Ribosomes are found in almost all organisms except viruses.  An E.coli cell may contain 15000 to 20000 ribosomes at any given time, but an active eukaryotic cell may have 10-20 times the number of prokaryotic cells.   

 Oocytes of certain amphibians’ posses’ three million ribosomes per cell and the same is stored for the future use.  While in prokaryotes, ribosomes are distributed through out the cell, eukaryotic cells contain different classes of ribosomes and they are located in different sites like cytoplasm, mitochondria and plastids.  Cytoplasmic 80s ribosomes are either bound to endoplasmic membrane or freely.  The majority of the so-called free ribosomes are found located in the intersection of microtrabacular(?) and actin filament network.  On the contrary cellular organelles like chloroplast and mitochondria contain another class of ribosomes called 70s, which are more or less similar to that of bacterial ribosomes.  In the Oocytes of chicks and lizards, ribosomes are aggregated on membranes into crystalline structures.  They remain inactive till they are required at some stage of development.

Class of ribosomes:

Ribosomes can be isolated by magnesium precipitation. If some ribosomes, obtained from a eukaryotic organism, are subjected to density gradient ultracentrifugation, ribosomes settle into two distinct bands.  Based on the sedimentation values, determined by Svedberg, they can be distinguished into 70s and 80s ribosomes.  The 80s ribosomes are found in cytoplasm, whereas 70s types are found in mitochondria and chloroplasts.  The 70s type are smaller and 80s are little larger.  However, prokaryotes contain only one kind of ribosomes i.e. 70 type.  The 80s and 70s ribosomes can be further distinguished by their sensitivity to chloramphenicol (CAP) and cycloheximide (CHI). The 70s ribosomal mediated protein synthesis is inhibited by chloramphenicol, while 80s ribosomal protein synthesis is inhibited by CHI.

Chemical composition:
Components of Ribosomes:

Types
RNA size
Number of proteins
Methylations
Functions
70 S ribosomes
 Coded by seven genes


30 or more methylations
30s subunits
16s RNA,
1540-42 ntds
21 (s1 to s21)
10 at 2’OH,
2,methyl adenines,
2,dimethyl guanines
Help in processing and folding
50S subunits
23s RNA,
2900 ntds;
5s RNA,
120 ntds
31, L1 to L31
20 at 2’OH of sugars

80S ribosomes:
Coded by hundreds of genes located on chromosomes12,13,14,21 and 22


>100 sites for methylations and 100 sites for pseudouridenylations
Yeast has 43 pseudo uridines
40S subunits
18s RNA;( 1843
Or 1900 ntds)
33;
S1 to s34
43 to 44 methylations at 2’OH groups, plus conversion of Uridine into pseudo-Uridines

60s subunits
28s-RNA;(4718- 4800 ntds);
5.8s RNA;(160ntds);
5s RNA;(120ntds);

49;
L1 to L45-50
74 methylations at 2’OH of sugars,
Methylation at adenine,
Methylation at guanine, plus conversion of Uridine into pseudo-Uridines

Mitochondrial ribosomes: 70s like (general);
Fungus-73s;
Maize-78s;
28s
12s
-1560 ntds,48 proteins
-29 proteins



Chloroplast ribosomes: 70s
16s RNA
23sRNA,
5s RNA,
4.5s RNA








Prokaryotic Ribosomal RNA and Riboproteins:


This figure shows 70S ribosomal subunits



This is simple diagram showing the possible secondary structure based on nucleotide sequences


              A simple diagram showing subunit components



  • Secondary structures of each of the rRNAs have been determined by their sequence analysis.  
  • The 16s rRNA and 23s rRNA, each of them, show four domains and  each of them are distinguished by the binding of specific riboproteins. 
  • The 16s RNA’s domain I starts from 5’ end progresses into domain II, III and IV in an order. 
  • At the 3’ end of the IV th domain of the 16s rRNA it has a small segment with a sequence that binds to the 5’ end of non coding Shine-Delgarno sequence which is a leader sequence of mRNAs.
  • The sequence is 3’ AUUCCUCCACUAG—5’.  
  • Similarly there are specific ribo-protein binding sites in each of the domains, ex. S4 & s20 bind to domain I, s8 7 & s15 bind to domain II, s7, 9,13 and 19 bind to domain III; thus each of the binding domain can be identified. 
  • Binding of tRNA and other factors to specific regions have been discerned by a variety of techniques such as electron microscopy, immuno labeling, neutron scattering techniques. 
  • Even eukaryotic subunit rRNAs show such domains identified by their ability to bind to certain riboproteins and other RNA species such as tRNA and other translational factors.
  • Some commonality of the sequence and secondary structures can be observed when one compares the 5’end of the 23s RNA of prokaryotes with that of 5’ ends of eukaryotic 5.8sRNA.  A secondary structure of rRNAs suggests the overall structural features of ribosomes.
  • It can be discerned that rRNAs from eukaryotes also show similar structural features.
    Assembly:

  • Assembly or association of riboproteins with rRNA is sequential and stepwise.
  • Methylation of 2’OH of ribose sugars and at adenine and guanine nucleotides at specific position is critical, and such methylations are performed by specific methylases and they use sequence driven secondary structures as motifs for identification of sites.



The ribbon diagram shows the positioning of tRNA on large ribosomal surface; A,P and E sites



Assembly of small ribosome subunits:
16sRNA + 16 s riboproteins à 21 s particles (can assemble at 20^oC),
21s particles + 6s riboproteins >à 26 s particles,
26 s particles ----> 30 s particles.

Assembly of Large Ribosome subunits:

23SRNA + 5sRNA -à 33 s particle,
33 s [articles -à 41 s particles,
41 s particles -à 50s particles


During dissociation also, certain subunits dissociates fast, even at the earliest steps of preparation; they are called split proteins. Such proteins are found both in small and large subunits.  Even during assembly, certain proteins associate at 0^oC, this is because great affinity of some proteins to certain RNA sequence.  Cold sensitive mutants block such assembly; they are called Subunit Assembly Defective mutants (SAD mutants).  Proteins, which associate, first are hard to disassociate and they are called core groups, and proteins, which assemble last, are the first to dissociate.  The following figure depicts sequential steps in the assembly.


rRNA          5’--------------------------------------------------------------------------3’
                       I          I           I        I
1st level                    I          s4      I    I     s8
2nd level                   s15     I          s20          s7
3rd level                         s17             s13
4th level      s16
5th level                         s12            s9  s19
6th level                   s18                              s5



Assembly sequence:
                    
30s =  17.5sRNAàs4,s8,s15-às1,s5,s7,s13--->s2,s3,s6,s9,s10
s17, s20        s16, s21   s11, s12, s14, s18/19

50s= 25sRNA--->L1,4,5,8,9,10---->L3,7,11,14-->L2, 6,12,10,28,31,32,
                     13,17,18,20, 15, 19, 23      
                     21,21,22,23,
                     24,25,27,29,
                     30, 33.

   30s [16s RNA]        O^oC        40^oC                  O^oC
+[ s21  proteins]--------------------> 21s--------------->26s------------->30s
                                 


50s [23sRNA]     o^oC               44^oC           O^oC          50^oC
+5sRNA+34L] ---------------->33s---------------->41s------------->48s----------->50s
Proteins]   

  • As the 5’ end of the precursor rRNA emerges during its synthesis, s4, 8 and 15 bind to this region tightly.  Then s17 and s7 join directly on to the RNA, later other proteins join by protein-protein or protein-RNA interactions.
  • Proteins s1, 3, 4,5,9,12,18 and the 3’ end of 16s RNA are involved in mRNA binding.
  • Peptidyl transferase function at P-site involve proteins L-2, 11, 15,16,18,23, and 27 in association with 23s RNA.
  • About 40 ntds long region of 16S RNA is located in the platform of 30s ribosomal subunit.
  • Peptidyl transferase occupies valley in the ribosome.
  • Two L7 and two L12 together act as GTPase.

Role of rRNA in protein synthesis (Prokaryotic):

  • In the molecular organization of ribosomes, both RNA and proteins are ordered and occupy certain specific invariant positions and perform specific function.  As a 3-D structure, it goes through several conformation changes with each binding events and catalysis.
  • The 3’ terminus 16s RNA of 30s ribosome directly interacts with 5’ end Shine-Delgarno sequence of mRNA and facilitates initial binding of it ribosomal surface so as to bring the first codon exactly to P site.
  • Specific regions of 16s RNA interact with tRNA for the binding at P and A sites.
  • 23 S RNA interacts with CCA terminus of peptidyl tRNA.
  • It is envisioned that there is RNA-RNA interaction and protein –protein interaction as well as protein-RNA interaction, thus both subunits are held together while they perform functions.
  • There must be some proteins, which perhaps act as motor proteins in moving ribosomes on single stranded mRNA in ATP dependent manner, similar to helicase.
  • Cleavage of 3’ region of 16S RNA by E3 Colicin abolishes initiation of translation.
  • Methylation of Adenine at 6th position and at 3’ end (di methylation to Adenine) of 16s RNA, facilitates dimrization of 30s and 50s units.  If methylases are absent dimrization fails.
  • Sensitivity to Kusugamycin depends upon methylation or absence of methylation at the above-mentioned sites.  Mutation at these sites abolishes sensitivity to the drug, but methylation at these sites makes it Kusugamycin resistant. 
  • Kusugamycin blocks initiation of translation by releasing F-met tRNA from ribosomal surface.
  • Mutation in the of 3’ end of 16s RNA suppress terminator codon function.
  • A mutation in rRNA can lead to frame shift function, because recognition between mRNA and rRNA doesn’t take place.
  • A region at 1400th ntds in 30s, is directly involved in the binding of peptidyl tRNA at P-site.
  • Both 16s and 23s RNAs are involved in organizing A and P site.
  • The CCA-end of tRNA at P- site protects 23SRNA from Rnase digestion.
  • The 23s rRNA is involved in organizing the exit site E, found in 50s subunit.
  • The 23s RNA is involved in catalyzing peptide bond formation; hitherto it is believed that an enzyme called di peptidyl transferase found in larger ribosomal subunit is involved in peptide bond formation.
    Ribosome Mediated Inhibitors of translation:

    Kusugamycin: initiation (PK), displace F-met tRNA, mutants lack methylation of 16 s rRNA at the 3’end.
    Streptomycin: initiation (PK), mutation in s12 of 30s ribosome causes resistance.
    Kirromycin:  elongation (PK), EF-Tu-GDP release is blocked by the antibiotic and no recycling.
    Puromycin:   elongation (PK), premature termination, because Puromycin has structure similar to tRNA configuration.
    Erythromycin: peptidyl transfer (PK), blocks peptide bond formation, mutation in 23sRNA results in resistance.
    Chloramphenicol: peptidyl transfer (PK), blocks peptidyl bond formation,
    Cycloheximide: translocation (EK), inhibits peptidyl transferase on 60s subunit.
    Fusidic acid:       translocation (PK),  EF-G-GDP cannot be released, no recycle.
    Thiostrepton: translocation (PK) binds to 23sRNA and inhibits GTPase activity.