Luciferase already works in plants. Good luck trying to read a book with it, though.

UCSD

Could we eventually do away with streetlights and have our neighborhoods bathed in the diffuse glow of self-lit trees? That's the premise behind a new Kickstarter campaign that has been featured on TXNOLOGIST and Slashdot. As of this writing, the project has already received more than double its goal of $65,000, with each donor being promised a glowing plant. Long-term, the project's leaders hope to expand out to trees, which is why their promotional video talks about doing away with streetlights.

There's just one small problem: as planned, the plants won't glow. At least not without a fertilizer that costs $200 a gram. Even if the team were to overcome this hitch, trees would probably never generate enough light to do away with a street lamp.

If you follow the biosciences, you'd be forgiven for thinking that glowing creatures were a dime a dozen. For example, researchers are regularly creating glow-in-the-dark mice and fish, and the technique has been used in a variety of species. But all of this work relies on the green fluorescent protein (GFP) and its relatives, which glow in other colors. GFP is great, and it's truly worthy of the Nobel Prize in Chemistry that its development was awarded. But bioluminescent animals only glow in the sense that black light posters do: they require UV light to excite the molecule, which then releases energy in the visible spectrum.

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The actin fibers of a nerve cell's growing axon are shown in red here.

NIH

The cells of our bodies aren't just featureless bags of proteins. Many of them have distinctive shapes and structures that are essential to their function. Neurons, for example, extend processes away from their cell bodies for up to several feet. The lining of your intestines has a specialized surface for absorbing food. And when immune cells encounter an infected cell, they form a specialized surface that allows them to kill the infected cell without harming its neighbors.

To form all of these structures, the cell has to be internally specialized, with different regions having distinct sets of proteins and chemicals. But it's hard to study the processes that make one part of the cell different from another. Most of the tools we have are rather blunt and affect the whole cell equally. But researchers have reported a clever trick that lets them activate proteins in a specific location: stick them on a tiny magnetic bead, then move the bead around inside the cell.

Cells usually form specialized structures in response to signals from their environment. Nerve cells receive signals from elsewhere in the body to direct where their axon grows, and immune cells recognize foreign proteins on the surface of other cells that help direct them to attack.

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Aurich Lawson / Thinkstock

The revolution in biotechnology has generated a lot of potential therapies that could avoid some of the problems of traditional medicine. Proteins manufactured in bacteria can supplement natural proteins; DNA-based vaccines can make immunity more specific while lasting for months at room temperature.

Most of these, however, haven't always worked out well in the real world. Proteins need to be injected to avoid the digestive system, but are often cleared from the blood quickly enough that repeated injections are needed. DNA vaccines work great, provided you can get the DNA into cells, which has turned out to be a significant technical hurdle.

Two papers, published this week, provide some indications of how researchers are working to get around these hurdles.

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The plant left behind after corn is harvested could be a source of both biofuels and the enzymes that create them.

LBL

So far, the first generation of biofuels is being made from things like corn, palm oil, and sugar cane. But only a small part of these plants—a part we'd already been using for other things—is actually made into fuel. Being able to make biofuels from the rest of the plant would allow us to get more from existing crops, use the leftover biomass from food production, and allow us to process plants that grow on marginal terrain.

Unfortunately, most of the carbon in a plant is locked up in cellulose, a very tough polymer made from simple sugar molecules. Before we turn a plant into biofuel, we need to figure out how to break down the cellulose. Right now, that process takes harsh conditions and long treatments with enzymes, which significantly adds to the cost. But some bioengineers at a company in Massachusetts have made a plant that carries an enzyme that can help digest itself—but the enzyme remains inactive until the plant is processed.

Hemicellulose is a major component of plant cell walls. Its presence helps protect cellulose from digestion, so digesting it not only liberates sugar for making biofuels, but it also makes the sugar in cellulose easier to access. Digesting away hemicellulose is thus a key early step in biofuel production, and requires either harsh chemicals or expensive enzyme treatments.

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USDAgov

In biology, researchers are usually pretty dismissive of experiments that result in only a single sample. When there's (as scientists put it) an "n of one," it's hard to tell whether the results are significant or a random fluke. But, in the case of a paper released on Monday by PNAS, the n happens to be a cow that carries a transgenic construct that knocks down the expression of a gene that encodes one of the major allergens found in milk. And the data that led to the cow makes a compelling case that the development is significant.

The work focuses on the β-lactoglobulin gene (BLG), which encodes a protein that's found in the milk of cows and other ruminants, but isn't produced by humans. That difference may be what makes it one of the major sources of milk allergies, which affect between two and three percent of infants born every year. Getting rid of the gene might make milk a viable option for more people, provided that doing so has no ill effects on the cows.

But deleting the gene is a real challenge. Unlike mice, where genes can be knocked out routinely, the techniques for elimination of genes and cloning of embryos in the cow are quite a bit less advanced. So, the authors turned to a different approach, called RNA interference. This involves designing short pieces of RNA that match sequences in the messenger RNA produced by the BLG gene, which allows them to base pair and form stretches of double-helical RNA. This keeps the messenger RNA from being translated into the BLG protein.

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Harvard University and Caltech

With billions of years of tinkering behind it, biology has a bit of a head start on engineers, creating materials like geckoes' feet and spider silk that have remarkable properties. So some materials researchers have studied biology's output in order to try to match its performance, with a few notable successes. Now, a team from Caltech and Harvard have put together a device that's a mixture of biological material and plastic, and tweaked their design until it could swim like a jellyfish.

Swimming like a jellyfish isn't necessarily the most useful ability to have, but the simplicity of the jellyfish body plan makes for a somewhat easier engineering problem, and makes for straightforward comparisons between the performance of the test construct and the real thing. Plus, the research team has set its sights pretty high, focusing on building a hybrid device that's part plastic, part biological material.

The rough outlines of jellyfish swimming are pretty well understood, but the authors focused on swimming details of juveniles of the species Aurelia aurita. The first step in this swimming motion is a contraction of the organism's bell; in Aurelia, this is driven by a single layer of muscle cells that line the interior of the organism's surface. Once these relax, the slow spreading out of the bell is drive by the mechanical properties of the bell itself, which drive the organism back towards forming a flat disk. Incidentally, this sweeps new water immediately beneath the bell itself, which helps the organism feed.

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