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Scientists determine
specific areas in protein structure
Science
responsible for inducing infectious nature of multi-complex
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research news
proteins associated with the cell’s skeletal network
Date: June 26,
2014
Source: College of Physicians and Surgeons of Columbia University
On the 16th day of May 2014, scientists of Colombia University, through rigorous experimental
trials and extensive research, have amassed success in pin-pointing specific regions of proteins,
which can induce self-replicating infectious agents that exert direct control on the movement of
protein producing cellular machinery to the cell’s skeleton like framework (Kandel et al., 2014).
Determining regions of specific amino acids that could potentially induce a prion-state protein
has had important implications in research concerning various factors that cause disease. The
findings of this study are significant because they have set the stage for researchers to delve
further into the field of cell pathology and determine the extent to which certain proteins can be
infectious, especially in the field of neuroscience.
In order to fully comprehend the significance of the claims and findings of this research, it is
necessary to describe a few key concepts in brevity.
Proteins are synthesized from genetic information, namely DNA and RNA, by the process of
translation (Freeman et al., 2013). They consist of long chains of subunit molecules known as
amino acids (Freeman et al., 2013). There are twenty major amino acids that occur naturally
within organisms, with each unique amino acid having a designated name such as methionine or
lysine (Freeman et al., 2013).
Amino acids can be further broken down into their component parts which consists of a
Nitrogen-based end, a Carbon-based end, and the rest of the molecule, also referred to as an ‘Rgroup’ or a ‘side chain’ (Freeman et al., 2013). There are three main classes of side chains which
vary in their molecular properties based on the interactions between certain atoms in the side
chain. These include nonpolar, polar, and electrically charged side chains (Freeman et al., 2013).
Proteins vary in both their folding into higher order structures and cellular function depending
heavily upon the linear connectivity of these amino acids, and consequently their unique side
chains (Freeman et al., 2013).
The aforementioned prions are misfolded proteins that are capable of inducing infection. They
are comprised of specific amino acid sequences, within the protein, which lack a certain level of
complexity maintained by electrically charged side chains (Kandel et al., 2014). Instead, prions
consist mostly of long sequences of polar, uncharged side chains, specifically glutamine and
asparagine, which affect misfolding of the protein as a whole (Kandel et al., 2014). Prions are
capable of multiplying because they can affect misfolding of properly folded proteins, thereby
triggering a chain reaction in which newly misfolded proteins can induce misfolding in other
normal proteins (Kandel et al., 2014). This results in a mass collection of infectious proteinbased particles that essentially clump together by the process of aggregation (Kandel et al.,
2014).
Modern
Science
©
Your source for current and reliable
research news
Moreover,
the
cytoskeleton is essentially similar to the
structure of the
human skeletal system in that it provides
structural support
for the cell and gives it shape (Freeman et
al.,
2013).
However, the cytoskeleton also plays a
major role in transporting various materials throughout the entire fluid matrix in the cell
(Freeman et al., 2013). Thus, the cytoskeleton is of utmost importance to the proper growth and
functioning of a cell, especially if that cell is specialized within a multicellular organism.
In this experiment conducted by
Kandel and his colleagues, two
proteins, namely Tia1/Pub1 and Sup35,
were of particular interest not only
because they contained “prion-rich
domains” but also for the reason that in
their normal state they are associated
with a cell’s cytoskeleton framework
(Kandel et al., 2014).
Line structures are a visual indication
that aggregation is occurring at the
molecular level (Kandel et al., 2014).
Figure 5B adequately represents the
influence of various prion regions,
found in both Sup35 and Tia1, on the
formation of line structures within the
cytoskeleton (Kandel et al., 2014).
Specifically, it conveys that the entire
‘N’ region and amino acids 166-220 in
‘M’ region, containing the previously
mentioned glutamine and asparagine
side chains, are both necessary to form
line structures as indicated by the
fluorescent images (Kandel et al.,
2014). These two domains, however,
are not sufficient to produce line
structures,
because
subsequent
fluorescent images depict that one
domain without the other does not
produce line structures in the cytoskeleton (Kandel et al., 2014). This pattern of line formation is
true for Sup35 and Tia1/Pub1 as indicated by the last two fluorescent images of the figure
(Kandel
et
al.,
2014).
This relates back to the process of aggregation by which infectious proteins clump together. In
the case of Tia1/Pub1 and Sup35, which are directly associated with the cell’s cytoskeleton,
aggregation would drastically disrupt the integrity of the cytoskeleton structure, thereby severely
hindering proper cell growth and functioning (Kandel et al., 2014).
Modern
Science
©
Your source for current and reliable
research news
On a small scale if
a few cells died it would not produce a
noticeable effect on a multicellular organism. However, imagine the drastic complications that
could occur if aggregation were to disrupt cytoskeleton structure of thousands of cells. This
would result in death of tissues which would consequently produce illness in the multicellular
organism, especially observed in various neurodegenerative diseases such as Alzheimer’s
(Kandel et al., 2014).
New discoveries integrating the research produced by the scientists of Colombia University
could one day identify new remedies for neurodegenerative disorders caused by prions.
References:
Freeman, S., Harrington, M., & Sharp, J. (2013). Biological Science (3rd ed., Vol. 1). Toronto,
Ontario: Pearson Learning Solutions.
Kandel, E., Li, X., Rayman, J., & Derkatch, I. (2014). Functional Role of Tia1/Pub1 and Sup35
Prion Domains: Directing Protein Synthesis Machinery to the Tubulin Cytoskeleton. Molecular
Cell, (55), 305-318.
Scientists determine
specific areas in protein structure
Science
responsible for inducing infectious nature of multi-complex
©
Your source for current and reliable
research news
proteins associated with the cell’s skeletal network
Date: June 26,
2014
Source: College of Physicians and Surgeons of Columbia University
On the 16th day of May 2014, scientists of Colombia University, through rigorous experimental
trials and extensive research, have amassed success in pin-pointing specific regions of proteins,
which can induce self-replicating infectious agents that exert direct control on the movement of
protein producing cellular machinery to the cell’s skeleton like framework (Kandel et al., 2014).
Determining regions of specific amino acids that could potentially induce a prion-state protein
has had important implications in research concerning various factors that cause disease. The
findings of this study are significant because they have set the stage for researchers to delve
further into the field of cell pathology and determine the extent to which certain proteins can be
infectious, especially in the field of neuroscience.
In order to fully comprehend the significance of the claims and findings of this research, it is
necessary to describe a few key concepts in brevity.
Proteins are synthesized from genetic information, namely DNA and RNA, by the process of
translation (Freeman et al., 2013). They consist of long chains of subunit molecules known as
amino acids (Freeman et al., 2013). There are twenty major amino acids that occur naturally
within organisms, with each unique amino acid having a designated name such as methionine or
lysine (Freeman et al., 2013).
Amino acids can be further broken down into their component parts which consists of a
Nitrogen-based end, a Carbon-based end, and the rest of the molecule, also referred to as an ‘Rgroup’ or a ‘side chain’ (Freeman et al., 2013). There are three main classes of side chains which
vary in their molecular properties based on the interactions between certain atoms in the side
chain. These include nonpolar, polar, and electrically charged side chains (Freeman et al., 2013).
Proteins vary in both their folding into higher order structures and cellular function depending
heavily upon the linear connectivity of these amino acids, and consequently their unique side
chains (Freeman et al., 2013).
The aforementioned prions are misfolded proteins that are capable of inducing infection. They
are comprised of specific amino acid sequences, within the protein, which lack a certain level of
complexity maintained by electrically charged side chains (Kandel et al., 2014). Instead, prions
consist mostly of long sequences of polar, uncharged side chains, specifically glutamine and
asparagine, which affect misfolding of the protein as a whole (Kandel et al., 2014). Prions are
capable of multiplying because they can affect misfolding of properly folded proteins, thereby
triggering a chain reaction in which newly misfolded proteins can induce misfolding in other
normal proteins (Kandel et al., 2014). This results in a mass collection of infectious proteinbased particles that essentially clump together by the process of aggregation (Kandel et al.,
2014).
Modern
Science
©
Your source for current and reliable
research news
Moreover,
the
cytoskeleton is essentially similar to the
structure of the
human skeletal system in that it provides
structural support
for the cell and gives it shape (Freeman et
al.,
2013).
However, the cytoskeleton also plays a
major role in transporting various materials throughout the entire fluid matrix in the cell
(Freeman et al., 2013). Thus, the cytoskeleton is of utmost importance to the proper growth and
functioning of a cell, especially if that cell is specialized within a multicellular organism.
In this experiment conducted by
Kandel and his colleagues, two
proteins, namely Tia1/Pub1 and Sup35,
were of particular interest not only
because they contained “prion-rich
domains” but also for the reason that in
their normal state they are associated
with a cell’s cytoskeleton framework
(Kandel et al., 2014).
Line structures are a visual indication
that aggregation is occurring at the
molecular level (Kandel et al., 2014).
Figure 5B adequately represents the
influence of various prion regions,
found in both Sup35 and Tia1, on the
formation of line structures within the
cytoskeleton (Kandel et al., 2014).
Specifically, it conveys that the entire
‘N’ region and amino acids 166-220 in
‘M’ region, containing the previously
mentioned glutamine and asparagine
side chains, are both necessary to form
line structures as indicated by the
fluorescent images (Kandel et al.,
2014). These two domains, however,
are not sufficient to produce line
structures,
because
subsequent
fluorescent images depict that one
domain without the other does not
produce line structures in the cytoskeleton (Kandel et al., 2014). This pattern of line formation is
true for Sup35 and Tia1/Pub1 as indicated by the last two fluorescent images of the figure
(Kandel
et
al.,
2014).
This relates back to the process of aggregation by which infectious proteins clump together. In
the case of Tia1/Pub1 and Sup35, which are directly associated with the cell’s cytoskeleton,
aggregation would drastically disrupt the integrity of the cytoskeleton structure, thereby severely
hindering proper cell growth and functioning (Kandel et al., 2014).
Modern
Science
©
Your source for current and reliable
research news
On a small scale if
a few cells died it would not produce a
noticeable effect on a multicellular organism. However, imagine the drastic complications that
could occur if aggregation were to disrupt cytoskeleton structure of thousands of cells. This
would result in death of tissues which would consequently produce illness in the multicellular
organism, especially observed in various neurodegenerative diseases such as Alzheimer’s
(Kandel et al., 2014).
New discoveries integrating the research produced by the scientists of Colombia University
could one day identify new remedies for neurodegenerative disorders caused by prions.
References:
Freeman, S., Harrington, M., & Sharp, J. (2013). Biological Science (3rd ed., Vol. 1). Toronto,
Ontario: Pearson Learning Solutions.
Kandel, E., Li, X., Rayman, J., & Derkatch, I. (2014). Functional Role of Tia1/Pub1 and Sup35
Prion Domains: Directing Protein Synthesis Machinery to the Tubulin Cytoskeleton. Molecular
Cell, (55), 305-318.
