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molecular chaperones

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Proteins consist of a set of Piau small molecules known as amino acids, a specific sequence of amino acids will ensure that the future can take a specific protein structure and function. The assemblage of various amino acids is carried out by molecular complexes known as ribosomes, the amino acid sequence formed proteins, however, are synthesized in the ribosomes simply linking to one another in sequence the various amino acids and thus initially consist of chains without a precise three-dimensional shape. Most of the protein chain wraps then spontaneously to take the final structure, the proteins tend to fold in such a way as to avoid ch nonpolar side chains of amino acids come into contact with the aqueous environment of the cell. Not all Portein can fold spontaneously, some are made up of hundreds of amino acids and must be helped to fold properly. the specific sequence of amino acids as we said it is important to allow the protena to fold into a specific shape and could take a specific functionality. If the withdrawal is not successful the feature is missing, or can be modified with deleterious consequences for the cell.




Cells can not wait passively proteins ripieghino correctly. Proteins are often incorrectly wrapped in apolar amino acids on the surface, rather than hidden in a safe in them. These non-polar hydrocarbon portions bind strongly with similar portions on other proteins and forming large aggregates. Random aggregates leading to the death cells: diseases such as sickle cell disease, mad cow disease, and Alzheimer's disease are caused by unnatural combinations of proteins that form fibrils which interfere with the cellular life.
Fortunately, the cell takes care of everything and there is a particular protein known as grppo Chaperon that guide other proteins during the process of proper folding. Protect them during the retreat shielded by other proteins that may bind and prevent the process. Many chaperone proteins are called "thermal shock" (with names such as HSP-60) because they are synthesized in large amounts when cells are exposed to strong heat, as in the case of burns. Too hot in general, destabilizes the protein and makes folding more often wrong. So when the temperature rises too much, the cells need extra help with their proteins.


The Chaperon HSP-60
This type of chaperone is complex and creates a closed environment for protein folding during which protects them completely during the process. An example is the complex GroEL- GroES of E.coli bacteria.
The structure consists of two overlapping rings of GroEL proteins, colored in green and blue, and a cap on the underside of GroES protein, colored red and yellow. As shown in the picture above, seven GroEL proteins form a ring with an internal cavity of the size of a protein. Proteins do not come wrapped up in this cavity and fold in it.

The Chaperon and HSP-70 chaperone prefoldin

Some smaller proteins that protect the ribosome have just left. At this stage the protein can have a very small percentage of their structure already folded, so the portions of the elongated chain with groups of non-polar hydrocarbon type are particularly susceptible to aggregation.

The chaperone HSP-70 (shown above) these portions is elongated, and there binds the fencing from the surrounding molecules. Then, with the energy of ATP, the chaperones release the chain when it is ready to fold. The HSP-70 are composed of two domains: one that binds ATP and controls the process, shown in the upper left from PDB 1dkg, and one that binds to portions of the protein chain is not wrapped in apolar hydrocarbon groups. A small peptide, colored pink, is tied in the deep cleft that binds the protein.

explore the structure

The large complex GroEL-GroES. In this figure three subunits have been removed GroEL in each ring to show the interior, leaving four subunits in each ring. In the two subunits on the back, hydrocarbon nonpolar amino acids LEU, ILE, VAL, MET, PHE, TYR and TRP are colored in blue. Note the strip of hydrocarbon hydrophobic amino acids near the entrance at the top. This interacts strongly with proteins do not fold luring them into the cavity. Now look at the lower cavity, capped by GroES in the bottom colored red. Using the energy of ATP (ADP is located in this structure, colored in red), the ring GroEL undergoes a great change in shape. The cavity becomes much larger, and the strip of hydrocarbon nonpolar amino acids is no longer in contact with the cavity. This means that a protein chain trapped inside (not shown) to close in on itself, having enough space for the process.

Sources:

PDB

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In life it takes courage

I learned to forgive, I have been able to go ahead, bite the bullet and be optimistic . I was haughty and proud at the right time and I was detained from making havoc of my dignity. When it came time to open my heart to a certain person, despite the idea terrified me , I gave free access to all my most intimate thoughts, without hiding or concealing anything. I was myself. I was vulnerable , because it would be just a simple word to destroy my protection, the force that even when I was immersed in the frustration and suffering could make sense of the struggle that I was fighting, a silent battle against myself, against my fears, against the world, against love, but above all against all rational behavior . A choice that they had all despised, seeing it as completely insane and wrong, has proved over time that the only ricucisse to sew the wounds that I wore on the heart. Today, thinking back to how I reacted in that situation, I can not help but be proud me and see how the courage, sensitivity and patience before or then always reward those who know how to use them in the right dose.

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The bacterium that utilizes the topoisomerase

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Here, the image on the right, the bacterium that if he had done so much talk in recent days. First, it must be said that all bodies to function properly, they must continually build new components for mobiles and it must be provided with a specific group of items. They are also known as macro-or macronutrients, because micro-organisms, but is also true of us, really in need in high quantities, are the elements that make possible the synthesis of carbohydrates, lipids, proteins, nucleic acids, etc. ... the elements are carbon (C), hydrogen (H), nitrogen (N), oxygen (O), sulfur (S), phosphorus (P). There are others, mostly ions, but these six elements are the skeleton of all organic molecules. Through this discovery, scientists say, although these elements are the building blocks of matter living, it is theoretically possible that other elements that we find on the periodic table can be effectively used in the same way.

The bacterium in question is a strain of gammaproteobacteria (GFAJ -1) which belongs to the family of Halomonadaceae. not yet understood because the microorganisms have a soft spot for arsenic. Evidently he has adapted to live in an environment where the presence of 'arsenic was very high, and therefore has learned to exploit both phosphorus and arsenic, but is yet to be proven. Oremland co-author of the discovery had already observed in the past that the bacteria in the lake, Mono Lake, full of arsenic, typically using this highly toxic reactions in photosynthesis, but no one had demonstrated the absorption of this element for internal use.

Wolfe-Simon and colleagues have collected mud and other sediments from Mono Lake and the bacteria have grown in the laboratory have taken then performed a series of dilutions intended to replace any remaining phosphate solution with higher and higher amounts of arsenic. They found that a type of microbe in the mix seemed grow faster than others.

They then radioactively labeled arsenate which was added in the culture medium so as to be able to monitor its distribution, it was observed that arsenic was present in the bacterium and was contained in proteins, lipids and metabolites such as ATP and glucose, as well as in nucleic acids that made up his DNA and RNA. The amounts of arsenic found were similar to those expected for the phosphate in normal cells, suggesting that the compound was used in the same way they would normally use the phosphate in the cell.

The team used two different techniques of mass spectrometry to confirm that the DNA of the bacterium contained arsenic, indicating that the item had assumed the role of phosphate in holding together the backbone of DNA. Further investigation have confirmed that the arsenate ion PERFORMED bonds with the carbon and oxygen in much the same way as the phosphate.

Now there are a number of questions you will answer. For example, if the phosphate content in kind as the ATP molecule was exchanged with arsenate, what effect it has on fnzioni important turning point in the cell? How can it be just as efficient? Metabolic processes in which arsenic would bind with glucose, if it is known that arsenic is more unstable in contributing to the formation of organic molecules, as it may be equally or similarly effective? And the phosphate groups bind to proteins and which play an important role in those changes of structure features of the latter? how can the exercise arsenate able to work effectively similmete? arsenate ion in fact similar in shape to the phosphate ion form bonds much weaker in water than those formed by the phosphate, is unstable, this means that they tend to break away and even though there may be other molecules that help stabilize these ties, the researchers would need to explain this discrepancy in the event standing. Yet, the discovery is "simply phenomenal" if you stand up after further chemical analysis, Benner added: "

means that many, many things are wrong in terms of how we see the molecules in the biological system."

SOURCES:

Nature, Scientific American , EurekAlert

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