TRANSLATIONAL CONTROL

&
POST-TRANSLATIONAL
MODIFICATIONS

Bhaskar Ganguly
Ph.D. , M.V.Sc., B.V.Sc. & A.H.

TRANSLATIONAL
CONTROL

PROKARYOTES
Structures formed by regions of the mRNA
obscure ribosome binding sites, thus reducing
translation of some cistrons relative to others.
Formation
of
stems
and
loops
inhibit
exonucleases and give certain regions of the
polycistronic mRNA a greater half-life.
Short antisense RNA molecules form duplexes
near the ribosome binding site of certain mRNAs.
Region of an mRNA has a tertiary structure that
resembles the binding site for a ribosomal protein
encoded by the mRNA. If there is insufficient
rRNA available for the translation product to bind
to, it will bind to its own mRNA and prevent
further translation.

EUKARYOTES
Two common strategies:
Varying the level of transcription of the gene
RNA processing
Presence of multiple copies of 5-AUUUA-3, usually in
the 3-noncoding region, marks the mRNA for rapid
degradation.
Masked mRNA: proteins bind directly to the mRNA
and preventing translation; mRNA can be translated
when the protein dissociates.
Non-coding sequences can cause mRNA to be located
in a specific part of the cytoplasm and, when
translated, can give rise to a gradient of protein
concentration across the cell.

Eukaryotes

micro RNAs bind to mRNAs to which they are

complementary, and either cause degradation
or translational repression of the mRNA
eIF4E inhibitory proteins prevents capdependent initiation of translation
small molecules, e.g. thiamine, can bind to
the ShineDalgarno sequence of prokaryotic
mRNAs and prevent ribosome binding

POLYPROTEINS
Bacteriophage and viral transcripts and many mRNAs
for hormones in eukaryotes (e.g. pro-opiomelanocortin)
are translated to give a single polypeptide chain that is
cleaved subsequently by specific proteases to produce
multiple mature proteins from one translation product.

PROTEIN MODIFICATION
The
modifications
include
acetylation,
hydroxylation,
phosphorylation,
methylation,
glycosylation and even the addition of nucleotides.
Hydroxylation of Pro is common in collagen, and
some of the histone proteins are often acetylated.

PROTEIN DEGRADATION
The N-terminal residue plays a critical role in
inherent stability.
Eight N-terminal amino acids (Ala, Cys, Gly, Met,
Pro, Ser, Thr, Val) correlate with stability (t 1/2 >
20 hours), eight (Arg, His, Ile, Leu, Lys, Phe, Trp,
Tyr) with short t1/2 (230 min) and four (Asn, Asp,
Gln, Glu) are destabilizing following chemical
modification.
Covalent linkage of molecules of the small,
highly conserved protein, ubiquitin, via its Cterminal Gly, to lysine residues in the protein.
Ubiquitinylated protein is digested by a 26S
protease complex (proteasome) in a reaction
that requires ATP.

THANK YOU