Kiss of Death

Sry Suryani W

 Definition of Ubiquitin
Ubiquitin: A small but extremely important protein that
acts the "kiss of death" to other proteins.
Ubiquitin consists of only 76 amino acids.
In the normal course of events, proteins are inactivated by
the attachment of ubiquitin to them, a process called
ubiquitination
Ubiquitin acts as a tag by which the protein-transport
machinery ferries a protein to the proteasome for
degradation.
Antagonizing this process are enzymes that remove
ubiquitin from proteins.
Ubiquitin is appropriately named since it is ubiquitous and
is present in virtually all types of cells. It is also one of the
most highly conserved (least changed) proteins during
evolution.
The amino acid sequence of ubiquitin is identical in all

 The cell functions as a highly-efficient

checking station where proteins are built
up and broken down at a rapid rate.
The degradation is not indiscriminate but
takes place through a process that is
controlled in detail so that the proteins
to be broken down at any given moment
are given a molecular label.

 This label has been called a "kiss of

death." The labelled proteins are then fed
into the cells' "waste disposers", the so
called proteasomes, where they are
chopped into small pieces and destroyed.
The kiss-of-death is ubiquitin. It fastens
to the protein to be destroyed,
accompanies it to the proteasome where
it is recognised as the key in a lock, and
signals that a protein is on the way for
disassembly. Shortly before the protein is
squeezed into the proteasome, its
ubiquitin label is disconnected for re-use.

 In 2004, Aaron Ciechanover and

Avram Hershko of the Technion Israel
Institute of Technology in Haifa, Israel
and Irwin Rose of the University of
California, Irvine, USA shared the
Nobel Prize in Chemistry "for the
discovery of ubiquitin-mediated
protein degradation."

 Proteasome: A protein degradation

"machine" within the cell that can
digest a variety of proteins into short
polypeptides and amino acids.
The proteasome is itself made up of
proteins. It requires ATP to work. It is
hollow and has openings at both ends
to allow entry of the protein to be
digested.

 A human cell contains about 30,000

proteasomes. These barrel-formed
structures can break down practically
all proteins to 7-9-amino-acid-long
peptides.
The active surface of the proteasome
is within the barrel where it is shielded
from the rest of the cell.

 The only way in to the active surface

is via the "lock", which recognises
proteins tagged with ubiquitin,
denatures these proteins and admits
them to the barrel for disassembly
,once the ubiquitin label has been
removed.
The peptides formed are released
from the other end of the proteasome.

 Proteasomes digest mainly

endogenous proteins, those
synthesized within the cell, as
opposed to extracellular proteins such
as the proteins in blood plasma.
The digestion of protein removes
excess enzymes and transcription
factors and supplies amino acids for
new protein synthesis.