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Molecule of the Month

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Ubiquitin

http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb60_1.html

“December 2004 Molecule of the Month 
  by David S. Goodsell
  Previous Features

“Nothing lasts forever. Many proteins, in fact, don’t last more than a few minutes. Our cells are continually building proteins, using them for a single task, and then discarding them. For instance, proteins that are used for signaling or control, such as transcription regulators and the cyclins that control division of cells, lead very brief lives, carrying their messages and then being thrown away. Specialized enzymes are also built just when they are needed, allowing cells to keep up with their minute-by-minute synthetic needs. This approach of planned obsolescence may seem wasteful, but it allows each cell to respond quickly to its constantly changing requirements.

Out with the Old

“Of course, cells need to control the destruction of their own proteins, making sure that they remove only proteins that aren’t needed any more. The small protein ubiquitin plays a central role in this job. Ubiquitin is attached to obsolete proteins, signaling to the cell that they are ready to be disassembled. As shown in the figure, a string of ubiquitin molecules (colored pink and tan here, from PDB entry 1ubq) is attached to old proteins, such as the src protein shown here (colored blue, from PDB entry 2src). The ubiquitin is then recognized by the destruction machinery of the cell.

Ubiquitous Ubiquitin

“As its name implies, ubiquitin is found in all eukaryotic cells and in cells throughout your body. The Nobel Prize in Chemistry was awarded this year to the three researchers who discovered its essential function in 1980. In the subsequent years, it has become apparent that apart from its role in protein disposal, ubiquitin is also used for other tasks, such as directing the transport of proteins in and out of the cell. By connecting ubiquitin together in short or long chains, or using different types of linkages between the molecules, many different signals may be encoded. Because of the important roles it plays, ubiquitin has changed very little over the evolution of life, so you can find a similar form in yeast cells, plant cells, and in our own cells. For more information on ubiquitin from a genomic perspective, see the Protein of the Month at the European Bioinformatics Institute.

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Ubiquitin may actually be the Molecule of the Millenium. The Hungarians like Soros are very interested. Coupled with an enzyme, ubiquitin may effectively bind and destroy specific target proteins. One of Project BioShields grantees, Veritas president George Oyler, is working on the properties of ubiquitin (c&p from the Project BioShield page):

#10, Veritas Inc, Rockville MD.
President George A. Oyler –medical license revoked for drugging and drinking, Nov.2003
http://www.mbp.state.md.us/forms/Nov_Dec03_sanctions.pdf ; 2009 – president of Synapic Research LLC, George A. Oyler http://www.synapticresearch.com/ , specializing in ubiquitin applications: “Ubiquitin is the subject of intense research in a number of biomolecular fields because researchers believe that control of ubiquitin could allow treatment of diseases by selectively destroying disease-causing proteins. Synapic Research is working to develop a “designer ubiquitin ligase” engineered to attach ubiquitin to a target protein of choice”…
UBIQUITIN
Veterinary Dictionary: ubiquitin
  “Heat shock (cell stress) protein present in mammalian cytosol; attaches to other cytosolic proteins and marks them for degradation either by specific proteases or by lysosomal enzymes.” http://www.answers.com/topic/ubiquitin
*
Heat shock protein basics: http://www.antigenics.com/products/tech/hsp/ ; “Although it was clear that animals could be vaccinated against cancer, for a long time it was not known how it worked. Then about 25 years ago, a graduate student named Pramod Srivastava began a series of experiments. He took tumor cells, broke them open, and separated the different parts of the cells into fractions. He then used each of the fractions as ‘vaccines’ to see which fraction protected the mice from developing cancer. After many experiments, he found that the element responsible for protecting the mice was heat shock proteins.”
Pramod Srivastava http://immune.uchc.edu/Lab%20pages/srivastava.htm; Mr. Srivastava founded the biopharmaceutical company Antigenics Inc. in 1994 with Garo H. Armen to exploit heat shock protein (HSP) technology. George Soros is a controlling owner of Antigenics Inc. http://www.halstedenterprises.biz/Pictures/Blogs/SorosCompanies.htm 
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Written by citizen2009

February 11, 2010 at 12:50 am

Posted in Uncategorized

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