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originally posted by: whereislogic
Epigenetic information is still contained within the DNA genome of an organism.
The information to produce proteins is also still contained within the DNA genome.
…‘Proteinaceous infectious particles’, or prions, exist stably in different conformational states, at least one of which can self-propagate over long biological timescales (Prusiner, 1982; Shorter & Lindquist, 2005). This endows prions with properties that are usually associated with nucleic acid-based elements of inheritance.
…In their native conformations, many yeast prion proteins regulate transcription, translation, and signaling networks (Halfmann et al., 2010). As a consequence, the prion states of these proteins can create diverse new traits. These can be beneficial, detrimental, or inconsequential, depending on the particular prion, genetic background, and environmental context (Shorter & Lindquist, 2005; True & Lindquist, 2000).
DNA is not dethroned.
The evolutionary motivated philosophy of junk-DNA and pseudogenes is (dethroned) though.
Remembering the Past:
A New Form of Protein-Based Inheritance
Intrinsically Disordered Proteins Drive Emergence and Inheritance of Biological Traits
Explain why you think epigenetic information is stored in RNA.
RNA-mediated epigenetic regulation of gene expression
Diverse classes of RNA, ranging from small to long non-coding RNAs, have emerged as key regulators of gene expression, genome stability and defence against foreign genetic elements. …These co-transcriptional silencing mechanisms form powerful RNA surveillance systems that detect and silence inappropriate transcription events, and provide a memory of these events via self-reinforcing epigenetic loops.
Nature Reviews Genetics 16, 71–84 (2015) doi:10.1038/nrg3863
Published online 02 January 2015
RNA Epigenetics
DNA isn’t the only decorated nucleic acid in the cell. Modifications to RNA molecules are much more common and are critical for regulating diverse biological processes.
…A variety of chemical modifications decorate the nucleic acids, increasing the alphabet of DNA to about a dozen known nucleotide variants. The alphabet of RNA is even more impressive, consisting of at least 140 alternative nucleotide forms. The different building blocks can affect the complementarity of the RNA molecules, alter their structure, and enable the binding of specific proteins that mediate various biochemical and cellular outcomes. …
The Scientist » January 2016 Issue
Epigenetics studies genetic effects not encoded in the DNA sequence of an organism, hence the prefix epi- (Greek: επί- over, outside of, around).[1][2] Such effects on cellular and physiological phenotypic traits may result from external or environmental factors that switch genes on and off and affect how cells express genes.[3][4] These alterations may or may not be heritable, although the use of the term epigenetic to describe processes that are heritable is controversial.[5]
Do you mean the drivers of epignnetic traits are contained in RNA? As in RNA determines when something needs to override genes and DNA?
Genes turn markers on and off just like prions can.
Genes appear to be permanent and persist through future generations.
Epigenetic traits are corrected through future generations as long as the external stresses revert to normal.
originally posted by: raymundoko
a reply to: soficrow
I kind of feel like an asshole because I agree with you completely. I just took issue with the title.
Chairman and CEO of Biotechonomy, Enriquez says that humanity is on the verge of becoming a new and utterly unique species, which he dubs Homo Evolutis. What makes this species so unique is that it "takes direct and deliberate control over the evolution of the species." Calling it the "ultimate reboot," he points to the conflux of DNA manipulation and therapy, tissue generation, and robotics as making this great leap possible.
We are already in the midst of minor improvements to the human body and mind; Enriquez gave examples of growing new tissues for successful transplant, programmable cells, and augmenting our abilities through robotics. As this trend accelerates, more and more aspects of the human experience, of the human life, will be capable of scientific manipulation. While some improvement may come post-birth, our understanding of DNA and biology may lead to something much bigger.
The term "prion" is derived from proteinacious infectious particle and refers to the pathogen that causes transmissible spongiform encephalopathies (TSEs).
This small infectious particle is a disease-causing form of a protein called cellular prion protein (PrPc). PrPc is mainly found on the surface of cells in the central nervous system, but it is also located in other bodily tissues. Although the specific role of PrPc is not clear, studies suggest that this protein plays a protective role in cells and helps them respond to oxygen deficiency.
A prion is composed of abnormally folded protein that causes progressive neurodegenerative conditions, with two of the most notable being Bovine spongiform encephalopathy (BSE or mad cow disease) seen in cattle and livestock and Creutzfeldt-Jakob disease (CJD) seen in humans. These mis-folded proteins do not multiply in the host organism that they infect. Instead, they affect the brain structure by acting as a template, inducing proteins with normal folding to convert to the abnormal prion form.
These newly formed mis-folded proteins, in turn, act as further templates for the conversion of more normal proteins, leading to an exponential accumulation of prions in the tissue of the central nervous system. These abnormally folded proteins form plaques which are thought to cause "entanglement" of neurofibrils and interfere with synapse function. The nerve cells are eventually damaged and lost, which causes tiny vacuoles to form in the brain. These give the brain a sponge-like appearance under the microscope, hence the term spongiform disease arose.
This leads to brain damage and the symptoms of prion disease, which include impaired brain function; changes in personality, memory and behavior; intellectual decline and movement abnormalities, particularly ataxia. These symptoms usually develop during adulthood and worsen over time, eventually causing death within several years or even a few months.
Prion features
Prions are so small that they are even smaller than viruses and can only be seen through an electron microscope when they have aggregated and formed a cluster. Prions are also unique in that they do not contain nucleic acid, unlike bacteria, fungi, viruses and other pathogens. Prions are therefore resistant to procedures that destroy pathogens by breaking down nucleic acid. Furthermore, because these particles are an abnormal version of a normal protein that is already coded for in the body, they do not trigger a host immune response, as other pathogens do.
The normal prion protein is thought to be made up of flexible coils referred to as alpha helices, but in the abnormally folded form, these helices are stretched out into densely packed structures called beta sheets. Cellular enzymes referred to as proteases can break down the normal protein, but prion proteins are resistant to this and subsequently accumulate in the brain tissue as they replicate.
Prion-like behavior can also be seen in some types of fungi. These fungal prions have been studied extensively to provide clues as to how prions affect mammals, although fungal prions are not harmful to their host. [whereislogic: this is the time to think about my comment about "spin" and why little mention is made of this rather significant difference between so-called "fungal prions" (like in yeast) and other prions that cause serious diseases in the OP; personally I'm thinking about whether the terminology prions is appropiate for both phenomena seeing that their effects are already so different, suggesting something else is going on in yeast and other fungi, unless they can just handle it better because of their other attributes]
Prion discovery
In the late1960's, research showed that the agent that causes sheep TSE or scrapie was highly resistant to being deactivated by ultraviolet and ionizing radiation, therapies that would usually destroy any pathogens that contained nucleic acid. However, the nature of these particles was still unclear and scientists made various suggestions including proteins, membrane fragments, small DNA viruses and polysaccharides.
Some researchers decided that whatever the nature of the agent was, it did not depend on nucleic acid to reproduce. In 1982, Stanley B. Prusiner from the University of California in San Francisco, published an article in Science demonstrating purification of the scrapie causing agent and he described a protein. Prusiner wrote in the article: "because the novel properties of the scrapie agent distinguish it from viruses, plasmids, and viroids, a new term "prion" was proposed to denote a small proteinaceous infectious particle which is resistant to inactivation by most procedures that modify nucleic acids." Prusiner’s discovery led to him being awarded the Nobel Prize in 1997.
Sources
www.cdc.gov...
www.nhs.uk/.../Introduction.aspx
www.uclh.nhs.uk/.../PriondiseaseFAQ.aspx
ghr.nlm.nih.gov...
www.bseinfo.org...
In their native conformations, many yeast prion proteins regulate transcription, translation, and signaling networks (Halfmann et al., 2010).
originally posted by: soficrow
a reply to: raymundoko
It is all truly elegant.
1. tastefully fine or luxurious in dress, style, design, etc.:
elegant furnishings.
2.
gracefully refined and dignified, as in tastes, habits, or literary style:
an elegant young gentleman; an elegant prosodist.
3.
graceful in form or movement:
an elegant wave of the hand.
4.
appropriate to refined taste:
a man devoted to elegant pursuits.
5.
excellent; fine; superior:
an absolutely elegant wine.
6.
(of scientific, technical, or mathematical theories, solutions, etc.) gracefully concise and simple; admirably succinct.
: showing good taste : graceful and attractive
: simple and clever
originally posted by: soficrow
DNA is dethroned as the exclusive determinant of inheritance, and as the primary one for “traits.”
originally posted by: soficrow
...aboriginal experiences with shape-shifting.
The normal prion protein is thought to be made up of flexible coils referred to as alpha helices, but in the abnormally folded form, these helices are stretched out into densely packed structures called beta sheets. Cellular enzymes referred to as proteases can break down the normal protein, but prion proteins are resistant to this and subsequently accumulate in the brain tissue as they replicate.
In addition to a “native” nonprion conformation...
...they occasionally fold into a prion conformation...These changes in conformation profoundly alter the functions of the proteins involved...
originally posted by: PhotonEffect
a reply to: soficrow
It's what Biotechonomy's CEO, Juan Enriquez, has dubbed Homo-Evolutis
Check out his TED talk - it's pretty fascinating stuff.
Bloomberg's Overview of Biotechonomy
Biotechonomy is a life science venture capital firm specializing in start-up and early stage entrepreneurial companies. The firm typically invests in companies in genomics-based energy, industrial and agricultural opportunities; companies with technologies that accelerate drug discovery and development; and businesses capable of improving the diagnosis and treatment of disease sectors.
Cyborgs actually do exist; 1. about 10% of the current U.S. population are estimated to be cyborgs in the technical sense, including people with electronic pacemakers, artificial joints, drug implant systems, implanted corneal lenses, and artificial skin.
2003: protein misfolding. At school it all sounded so simple — transcription turns DNA into RNA, and translation of RNA gives you protein. …
…A huge variety of previously unrelated diseases, such as prion diseases, diabetes and cancer, share the pathological feature of aggregated misfolded protein deposits. This suggests the exciting possibility that these 'protein-misfolding diseases' are linked by common principles…
Trends Biochemistry, 2006: Intriguing recent data suggest that other protein misfolding disorders might also be transmitted by a prion-like infectious process.
Nature, 2016: Prions
Prions are an infectious protein usually referring to the protein in mammals called prion (PrP), but the term prions or scrapie protein can be generically applied to any protein that exhibits the same properties of taking on a misfolded conformation (PrPsc form) and templating and propagating further misfolding that leads to its infectivity.
Prions are proteins that convert between structurally and functionally distinct states, at least one of which is self-perpetuating. The prion fold templates the conversion of native protein, altering its structure and function, and thus serves as a protein-based element of inheritance.
…. Prions were originally identified as the cause of several rare neurodegenerative diseases in mammals, but the last decade has brought great progress in understanding their broad importance in biology and evolution. Most prion proteins regulate information flow in signaling networks, or otherwise affect gene expression. Consequently, switching into and out of prion states creates diverse new traits – heritable changes based on protein structure rather than nucleic acid.
…prions (have) properties that are usually associated with nucleic acid-based elements of inheritance. …
….Prion-based inheritance is highly orchestrated. …
many yeast prion proteins regulate transcription, translation, and signaling networks (Halfmann et al., 2010). As a consequence, the prion states of these proteins can create diverse new traits. These can be beneficial, detrimental, or inconsequential, depending on the particular prion, genetic background, and environmental context …
originally posted by: soficrow
a reply to: whereislogic
Your “prions only cause disease” reference is from the CDC’s Biosafety Manual.
In their native conformations, many yeast prion proteins regulate transcription, translation, and signaling networks (Halfmann et al., 2010).