Signal Peptide.

Juan Jesus Chavez Reyes.

Centro Universitario de Ciencias de la Salud (CUCS), Sierra mojada No. 950, Col. Independencia Oriente, C.P.44343,
Guadalajara, Jalisco, Mxico.
Email: juan_jesus_14dev@hotmail.com

Abstract:
The peptide signal plays an important role in targeting peptide prediction and prediction of subcellular
protein and protein translocation in both prokaryotic localization in general. After the first method for signal
and eukaryotic cells. This transient, short peptide peptide prediction was published by von Heijne,
sequence functions as a postal address in an 19862, more and more methods have emerged,
envelope by the orientation of the secretion of although not all methods have been publicly
proteins or for transfer to specific organelles for available.
further processing. Understanding how signal
peptides function is crucial in predicting which
proteins are translated and the function of these.
Signal peptides are found in proteins that are targeted
Structure
to the endoplasmic reticulum and eventually destined A signal peptide is made up of about 5 to 30 amino
to be either secreted/extracellular/periplasmic/etc., acids which are placed in a particular order and are
retained in the lumen of the endoplasmic reticulum, of the first to appear when the polypeptide chain is being
the lysosome or of any other organelle along the synthetized. The signal peptide decides on the fate,
secretory pathway or to be I single-pass membrane the transport route and the secretion efficiency of a
proteins. protein.3
A signal peptide (depending on the protein secuence,
eukaryote) has three distinct regions. First the n-
Introduction: region that has positively charged amino acids (Lys,
Arg, His) or negative (Asp, Glu), then the h-region that
The importance of signal peptides was demonstrated is hydrophobic and finally the c-region with the site
in 1999 when Gnter Blobel received the Nobel Prize recognition by signal peptidase (SPase).4
in Physiology and Medicine for his discovery that
"proteins have intrinsic signals that govern their
transport and location in the cell. He noted the
importance of defined peptide motifs to drive proteins
to their site function.
Ilustration 1: Schematic representation of a signal peptide.
Thousands of articles have been published
considering signal peptides, secretion and subcellular
localization, including knowledge of the use of signal
peptides as vehicles for chimeric proteins for the
biomedical and pharmaceutical industry. Many
articles describe statistical or machine learning
methods for signal
 Types of Signal Peptides
Most cell types and organisms employ various forms
of protein targeting to the extracellular environment
and to subcellular locations. Most of the proteins
directed to the extracellular space or to subcellular
locations carry specific sequence motifs (signal
peptides) that characterize the type of secretion /
targeting they experience.5
During the past few years a number of new signal
peptides or targeting signals have been found, and
the articles frequently describe a small amino acid
motif required for the secretion of a particular protein.
In most of the more recent cases, the motif of the
identified sequence is only found in this particular
protein and as such, can not be described as a group
of signal peptides.6
There are many different kinds of orientation signs.
One of the frequency signals is formed by short,
transient peptides known as signal peptide
sequences or leader, which are generally found in the
amino terminal secreted proteins. Signal peptides are
present in both prokaryotic and eukaryotic cells, with
indication of their universal ancient origin. They
function as a postal address in an envelope of
orientation labels by the secretion of proteins to
specific organelles or for further processing. The
signal peptides are degraded cleaved and take off
upon reaching their targeting locations. Interestingly,
not all proteins possess signal peptides, suggesting
that other mechanisms of protein targeting exist.7 1 3
"Address tags" or "Zip codes"
Each protein carries in its structure the necessary
information that specifies its proper location in the
cell. Specific amino acid sequences (topogenic
signals) determine whether the protein will pass
through the membrane into a particular organelle, will
be integrated into the membrane, or will be exported
outside the cell.8
Different signals have now been identified that direct
the proteins to different parts of the cell. These signs
can be compared to postal addresses or postal
districts that ensure that the traveler's luggage arrives
at the correct destination or that the letter arrives at
the correct postal address. These signaling
sequences are in fact a chain of different amino acids
present in the form of a short "tail" at one end of the
protein, or occasionally located inside the protein.9
Signal Peptide in action
Each protein is unique because each of them is
formed by a particular sequence of amino acids,
which is encoded in the genetic material (DNA) of the
cell. This sequence not only gives the protein its
physicochemical and functional properties, but
particular regions of this sequence constitute a true
'zip code' that determines the final destination and
location of each protein. This zip code is represented
by a region of the sequence commonly constituted by
the first 15 to 60 amino acids of a protein called signal
peptide or by a three-dimensional zone formed by the
interaction of several discontinuous regions of the
sequence of amino acids that are spatially associated
when Protein bends over itself, called patch signal.
Assembling the amino acid sequence, which will
constitute the primary structure of any protein, begins
in the ribosomes, which are subcellular structures
capable of reading the message that has been
transcribed from the DNA to RNA molecules, and
then add one by one The amino acids in a particular
sequence for each type of protein.10
This is how proteins whose first destination is the
endoplasmic reticulum have a signal peptide at their
amino terminal end that includes a sequence
composed of 5 to 10 hydrophobic amino acids that is
recognized by a receptor of this organelle that opens
a channel in Its membrane allowing such proteins to
cross it. Most of these proteins will then follow their
course to the Golgi apparatus, but those that also
have a certain sequence of four amino acids (-Lys-
Asp-Glu-Leu-COOH) at their other end (terminal
carboxyl) are retained In the endoplasmic reticulum
as proteins of this organelle.11
On the other hand, the signal peptide of the proteins
that will be destined for mitochondria contains several
short strokes of hydrophobic amino acids separated
by a positively charged amino acid. Proteins intended
for peroxisomes have a sequence of three specific
amino acids (-Ser-Lys-Leu-) near their carboxyl
terminus. While those destined to enter the cell
nucleus have a group of 5 or 6 positively charged
amino acids (Pro-Gly-Lys-Lys-Lys-Arg-Lys-Val-)
found inside the polypeptide chain. This entry to the
cell nucleus occurs through the pores of the nuclear
membrane and is mediated by other proteins known
as transport factors, among which keriophrine-beta2
is highlighted, which binds to the proteins to be
transported and directs Towards the nuclear
pores.10,11
8. Kll, Lukas; Krogh, Anders; Sonnhammer,
Erik L. L. (2004). "A Combined
Transmembrane Topology and Signal
Peptide Prediction Method". J. Mol. Biol.
338: 10271036.

9. von Heijne, G.; Gavel, Y. (Jul 1988).

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