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RIBOSOMES

The ribosome are macromolecules which are found within the cells.
Responsible for performing various biological functions like biological
protein synthesis also called as mRNA Translation. The ribosomes
consists mainly of 2 sub- units : the small and the large ribosomal sub
unit. Both the sub units consists one or more ribosomal RNA or rRNA
molecules and many other ribosomal proteins also called as RPs or R
Proteins. The ribosomes along with their associated molecules are
combined called as translational apparatus.

Discovery of Ribosomes

Ribosomes were first discovered in the mid 1950s by a cell biologists


from Romainan American background named GEORGE EMIL PALADE.
He initially named them Palade Granules because they were present in
granular form. However, the term ribosome was then coined by an
American biophysicist named HAROLD DINTZIS in the year 1958.

Structure of Ribosome

The ribosomes are considered as complex cellular machine. They are


largely made up of a specialized type of RNA called as Ribosomal RNA or
rRNA and as discussed above various proteins also. The two sub units of
ribosome that is large and small sub unit they fir together and work as
one single unit to translate the mRNA into the polypeptide chain during
the synthesis of protein.
The prokaryotic ribosomes are about 20 nanometers in its diameter.
They are composed of 65% rRNA and 35% ribosomal proteins. The
ribosomal sub units of prokaryotes and eukaryotes are much alike.
Svedburg is the unit of measurement used to describe the ribosomal sub
units along with RNA fragments. This is exactly why the units do not add
up correctly. For example the 70S ribosome is made up of 50S and 30S
sub unit.
The 70S ribosomes consists of a smaller sub unit which is 30S and a
larger sub unit 50S. The smaller sub unit that is 16S RNA sub unit
consists 0f 1540 nucleotides which are bound to 21 ribosomal proteins.
Where as the larger sub unit is composed of 5S RNA sub unit with 120
nucleotides and a 23S RNA sub unit with 2900 nucleotides and 31
proteins.

Archaeal Ribosome they share similar dimensions to the bacteria ones


and similarly 70S RNA ribosome made up of 50S larger sub unit along
with 30S smaller sub unit and three rRNA chains. However, this does not
apply any relation between Archaea and Bacteria.

Eukaryotic ribosomes are about 25 to 30 nanometers in diameters with


rRNA to protein ratio around 1. Eukaryotes have 80S ribosomes which
are found in cytosol which are made of two sub units the larger one being 60S ant
the smaller one being 40S. The smaller sub unit 40S containing 18S RNA
with 1900 nucleotides along with 33 proteins and the larger sub unit
containing 5S RNA with 120 nucleotides , 28S RNA with 4700 nucleotides
and 5.8S RNA with 160 nucleotides and a total of 49 proteins.

Functions of ribosomes

Ribosomes are termed as minute particles consisting of RNA and few


associated proteins which functions to synthesize proteins. Proteins are
very much important for many cellular functions for example repairing
damage or directing any chemical process. In the cell the ribosomes are
found floating in the cytoplasm or can be seen attached to the
endoplasmic reticulum. The main and the most important function of
the ribosoms is to convert the genetic code into any particular amino
acid and to build protein polymers from the amino acid monomers.
Ribosomes also acts as a catalyst in two very crucial biological processes
which are peptidyl transfer or peptidyl hydrolysis.
Translation

step in gene expression. The mRNA is "read" according to the genetic


code, During translation which is also considered as the second most
important which relates the DNA sequence to the amino acid sequence
in proteins . Each group of three bases in mRNA constitutes a codon, and
each codon specifies a particular amino acid (hence, it is a triplet code).
The mRNA sequence is thus used as a template to assemble in order the
chain of amino acids that form a protein. The mRNA leaves the nucleus
and travels to the cytoplasm where the ribosome is located. The
ribosomal sub unit contains various proteins and specialized RNA
molecules Ribosomal RNA or rRNA and transfer RNA or tRNA.
The tRNA molecules are called adaptor molecules because their one end
helps in reading the triplet code in the mRNA with help of
complementary base pairing where as the another end attaches to the
specific amino acid. The base paring is facilitated when mRNA and
amioacyl tRNA complexes are held together closely.
The translation of mRNA begins with the formation of a complex on the
mRNA present. There are three initiation factors which are named as IF1 ,
IF2 and IF3 they all bind to the smaller sub unit of ribosome. This forms a
pre initiation complex along with a methionine carrying tRNA which
binds to the mRNA near the start codon or AUG or ATG. Although
methionine is the first amino acid to incorporated or start the
translation process it is not considered as first amino acids in mature
proteins. A large number of proteins contains formylmethionine.
Once the initiation complex is formed the larger sub unit binds to this
complex which results in releasing or removal of the three initiation
factors. The large sub unit has three sites at which the tRNA molecules
comes and binds to it. There is A or amino acid at which the amioacyl
tRNA anticodon forms pairs with mRNA codon which ensures that
correct amino acid is added to growing polypeptide chain. Then there is
P site or polypeptide site where the amino acid is transferred to from its
tRNA to the growing polypeptide chain. And lastly there is an E site or
also called as and Exite site tRNA rests before being released back to the
cytoplasm for it bind to another amino acid and repeat the entire
process again. The initiator methionine tRNA is the only aminoacyl-tRNA
which is capable of binding in the P site of the ribosome, and the A site
is aligned with the second mRNA codon.
The next phase in translation is known as the elongation phase . Firstly ,
the ribosome moves along with the mRNA in the 5'-to-3'direction, which
needs the elongation factor G, in a process named translocation. The
tRNA that corresponds to the second codon can then bind to the A site,
a step that requires elongation factors (in E. coli, these are called EF-Tu
and EF-Ts), as well as guanosine triphosphate (GTP) as an energy source
for this particular process. After binding of the tRNA-amino acid complex
in the A site, GTP is cleaved to give rise to guanosine diphosphate (GDP),
then released along with EF-Tu to be recharged by EF-Ts for the next
cycle.
Next, peptide bonds between the now-adjacent first and second amino
acids are formed via a peptidyl transferase activity. For many years, it
was thought that an enzyme catalyzed this particular step, but recent
evidence indicates that the transferase activity is a catalytic function of
rRNA. After the peptide bond is formed, the ribosome shifts, or
translocates, again, thus causing the tRNA to occupy the E site again. The
tRNA is then released to the cytoplasm to pick up another amino acid int
eh cytoplasm. In addition, the A site is now empty and ready to receive
the tRNA for the next codon and synthesis.
This process is repeated until all the codons in the mRNA have been read
by tRNA molecules, and the amino acids attached to the tRNAs have
been linked together in the growing polypeptide chain in the
appropriate order. At this point, translation must be terminated, and the
nascent protein must be released from the mRNA and ribosome.

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