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A study just broke out of Tokyo that says some eyebrow-raising things about water bears and their DNA.
X-rays are a form of electromagnetic radiation, as are radio waves, infrared radiation, visible light, ultraviolet radiation and microwaves. One of the most common and beneficial uses of X-rays is for medical imaging. X-rays are also used in treating cancer and in exploring the cosmos.
X-rays are roughly classified into two types: soft X-rays and hard X-rays. Soft X-rays fall in the range of the EM spectrum between (UV) light and gamma-rays.
Soft X-rays have comparatively high frequencies — about 3 × 1016 cycles per second, or hertz, to about 1018 Hz — and relatively short wavelengths — about 10 nanometers (nm), or 4 × 10−7 inches, to about 100 picometers (pm), or 4 × 10−8 inches. (A nanometer is one-billionth of a meter; a picometer is one-trillionth of a meter.)
Hard X-rays have frequencies of about 1018 Hz to higher than 1020 Hz and wavelengths of about 100 pm (4 × 10−9 inches) to about 1 pm (4 × 10−11 inches). Hard X-rays occupy the same region of the EM spectrum as gamma-rays. The only difference between them is their source: X-rays are produced by accelerating electrons, while gamma-rays are produced by atomic nuclei.
Tardigrades are notable for being the most resilient animal: they can survive extreme conditions that would be rapidly fatal to nearly all other known life forms.
They can withstand temperature ranges from 1 K (−458 °F; −272 °C) (close to absolute zero) to about 420 K (300 °F; 150 °C), pressures about six times greater than those found in the deepest ocean trenches, ionizing radiation at doses hundreds of times higher than the lethal dose for a human, and the vacuum of outer space.
They can go without food or water for more than 30 years, drying out to the point where they are 3% or less water, only to rehydrate, forage, and reproduce.
“We had no idea that an animal genome could be composed of so much foreign DNA,” said co-author Bob Goldstein, faculty in the biology department in UNC’s College of Arts and Sciences. “We knew many animals acquire foreign genes, but we had no idea that it happens to this degree.”
(a) Subcellular localization of Dsup-GFP fusion proteins transiently expressed in HEK293T cells. Nuclear DNA was visualized by Hoechst 33342. Scale bars, 10 μm.
(b) Mobility shift of DNA by bacterially expressed Dsup protein in a dose-dependent manner (10, 50, 75 or 100 ng). Black arrowhead indicates the predicted size of the probe DNA (3 kbp, 10 ng). Red arrowhead indicates the position of the extremely slowly migrating DNA in the presence of Dsup protein. A similar extensive mobility shift was observed with histone H1.
First author Thomas Boothby, Goldstein and their collaborators revealed that tardigrades acquire about 6,000 foreign genes primarily from bacteria, but also from plants, fungi and Archaea, through a process called horizontal gene transfer – the swapping of genetic material between species as opposed to inheriting DNA exclusively from mom and dad.
Previously another microscopic animal called the rotifer was the record-holder for having the most foreign DNA, but it has about half as much as the tardigrade. For comparison, most animals have less than one percent of their genome from foreign DNA.
When the results of the sequencing came back, the Tokyo researchers found that the tardigrade genome was composed of more like 1.2% foreign DNA, which is a far cry from a sixth of the thing’s genes coming from lateral gene transfer. In their paper, they politely refer to the previous, possibly adulterated results as a “draft genome.”
The Tokyo University researchers were even able to watch the protein go about its work by tagging parts of the tardigrade genome with green fluorescent protein (GFP) and then watching as the protein migrated through cells in culture.
The damage-suppressing protein, Dsup, is closely associated with nuclear DNA; the scientists found it in the chromatin fragment of their cream-of-tardigrade soup. Chromatin is sort of like the options page of the DNA molecule, in that it determines which parts of the DNA molecule are transcribed.
When the team treated human cells in culture with extract of tardigrade, the GFP-tagged proteins stuck to human DNA just like they stick to tardigrade DNA, and cheerfully started doing what they do best: tamping down oxidative stress.
When X-rays hit human cells, they do two kinds of damage. X-rays can cause direct DNA strand breaks, which are mostly single-strand. When they strike water molecules, they can also excite them into producing reactive oxygen species, which also cause single-strand breaks. High enough doses of X-rays can cause double-strand breaks.
The damage-suppressing protein Dsup went immediately to work on the culture of human cells, suppressing or repairing single-strand and double-strand breaks by about 40%.
The federal government announced plans Thursday to lift a moratorium on funding of certain controversial experiments that use human stem cells to create animal embryos that are partly human.
Tardigrades, also known as water bears, are small aquatic animals. Some tardigrade species tolerate almost complete dehydration and exhibit extraordinary tolerance to various physical extremes in the dehydrated state.
Here we determine a high-quality genome sequence of Ramazzottius varieornatus, one of the most stress-tolerant tardigrade species. Precise gene repertoire analyses reveal the presence of a small proportion (1.2% or less) of putative foreign genes, loss of gene pathways that promote stress damage, expansion of gene families related to ameliorating damage, and evolution and high expression of novel tardigrade-unique proteins.
Minor changes in the gene expression profiles during dehydration and rehydration suggest constitutive expression of tolerance-related genes. Using human cultured cells, we demonstrate that a tardigrade-unique DNA-associating protein suppresses X-ray-induced DNA damage by ~40% and improves radiotolerance. These findings indicate the relevance of tardigrade-unique proteins to tolerability and tardigrades could be a bountiful source of new protection genes and mechanisms.
Two recent studies on long-lived seabirds demonstrate that the role of telomeres is far from being understood . In 2003, scientists observed that the telomeres of Leach's storm-petrel (Oceanodroma leucorhoa) seem to lengthen with chronological age, the first observed instance of such behaviour of telomeres.[34] In 2006, Juola et al.[35] reported that in another unrelated, long-lived seabird species, the great frigatebird (Fregata minor), telomere length did decrease until at least c.40 years of age (i.e. probably over the entire lifespan), but the speed of decrease slowed down massively with increasing ages, and that rates of telomere length decrease varied strongly between individual birds. They concluded that in this species (and probably in frigatebirds and their relatives in general), telomere length could not be used to determine a bird's age sufficiently well. Thus, it seems that there is much more variation in the behavior of telomere length than initially believed. Furthermore, Gomes et al. found, in a study of the comparative biology of mammalian telomeres, that telomere length of different mammalian species correlates inversely, rather than directly, with lifespan, and they concluded that the contribution of telomere length to lifespan remains controversial.[36] Harris et al. found little evidence that, in humans, telomere length is a significant biomarker of normal aging with respect to important cognitive and physical abilities.[37] Gilley and Blackburn tested whether cellular senescence in paramecium is caused by telomere shortening, and found that telomeres were not shortened during senescence.[38]
originally posted by: Teikiatsu
It'd be interesting to see if those proteins could repair the telomeres in our DNA. Those are the 'caps' on the strands, kind of like the hard plastic tips on shoelaces. Over time the telomeres break down from repeated replications which leads to damage of the main DNA strands segments.
Keep the telomeres healthy longer, the DNA stays stable longer.
originally posted by: chr0naut
originally posted by: Teikiatsu
It'd be interesting to see if those proteins could repair the telomeres in our DNA. Those are the 'caps' on the strands, kind of like the hard plastic tips on shoelaces. Over time the telomeres break down from repeated replications which leads to damage of the main DNA strands segments.
Keep the telomeres healthy longer, the DNA stays stable longer.
The tips to our shoelaces are called aglets.
One also might question the direction, genetically, of repairs to our telomeres as the DNA is gone, there is no structure upon which to base the repaired strand.
originally posted by: Teikiatsu
Keep the telomeres healthy longer, the DNA stays stable longer.