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WATCH: Sheffield flower arranger hosts virtual Glastonbury ‘gig’ from own home




For the last four years, Emma McGeehan, 42, of Abbeydale, has been running flower arranging workshops from Glastonbury’s ‘green fields’ site, where festival-goers can learn new skills in a sustainable and environmentally-friendly way.

However, when this year’s annual performing arts extravaganza was cancelled due to coronavirus, she instead recorded the workshop in her front room in Sheffield.

The tutorial was then shared on the festival’s website where it has since been watched hundreds of times by keen craftspeople unable to make their yearly pilgrimage to Worthy Farm.

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She said: “This would have been my fourth year of doing it and we normally run workshops for hundreds of people over the weekend.

“All the flowers we use are from Yorkshire. People choose the ones they want and we show them how to make a flower crown.

“But this year because of coronavirus they asked me to do it online. They wanted it to have a very ‘at home’ feel so I did it in my living room.”

As well as flower arranging, other workshops offered in the virtual green fields over the weekend included willow weaving, perfume making and hat designing.

A ‘floral crown’ design made in one of Emma McGeehan’s workshops.

“It is such a wonderful atmosphere and we fit the ethos of the festival really well,” said Emma.

“People always come up with weird and wonderful creations and we only work 10-4 every day so we have the rest of the festival to enjoy for ourselves.”

Glastonbury 2020 – which was due to be the festivals 50th anniversary – would have taken place between June 26-28 but was cancelled in March due to the coronavirus pandemic. It will return again in 2021.

As well as teaching flower arranging, Emma also works as a florist and provides flower designing services to weddings and other events including decorating bars for gin brands.

A ‘floral crown’ design made in one of Emma’s workshops.

Her studio – Orchis Floral Design – is based at Hagglers Corner on Queens Road and she can be contacted via her website at

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Elegant little vibe for gig




Little Village is back with a bang for the people of the South West, throwing a small party with a big line-up including Nathan Parsons, Chloe Payne and Josh Garner.

The elegant event at Driftwood Estate will celebrate local musicians and a return to live music post-COVID-19.

Parsons is back in Australia after journeying to Europe to work in a studio in Austria with new label Aton on two solo projects, including one acoustic and one electronic.

His music was inspired by the ocean, mountains and deep emotion, and he said his time in Austria had led him to miss the wild waters of the South West.

“I’ve been working pretty hard before the coronavirus hit and was going to release an EP over there,” he said.

Unfortunately, the COVID-19 situation in Europe deteriorated and Parsons made the difficult decision to come home to complete his latest single Follow the Ocean.

“I was working with some American artists and European artists collaborating on some rap songs, but I ended up getting signed after the label approached me when I was busking on the side of the street,” he said.

“We went to the studio to write a few songs and now one is ready for release.”

Parsons finished Follow the Ocean in the South West and sent it back to the label to be mixed and mastered by Scandinavian music wizard Felix Sterzinger.

“I wrote it based on being overseas away from friends and family. It was difficult going from chasing the summer to having three years of winter,” he said.

“Emotionally for me, its been about finding peace after missing the ocean. I found creativity from snowboarding some of the highest peaks in the world in Austrian mountains at minus 20 degrees,” he said.

Parsons is excited to return to the Little Village stage after previously performing at the intimate shows as part of duo Salt Tree. “I think the Little Village events are really unique, the organisers tend to make it a more artistic scene for the audience,” he said.

“You never really know what to expect when you play or attend those events.

“They’ll have couches and rugs for you to chill out on the grass, but it’s a stylish and a nice warm vibe. It’s definitely a very unique experience.”

Due to COVID-19 restrictions the July 16 event will be capped at 100 tickets.

Organisers and punters are also required to strictly adhere to social distancing and hygiene practices.

Tickets are on sale at

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Histones’ secret enzyme gig may have helped power eukaryote evolution





Credit: Science

Histone proteins (orange, blue, green, and purple) act as a spool to wind up DNA (white). Two key amino acids (histidine 113 and cysteine 110) in the H3 histone protein (orange) can bind and reduce copper ions.

In our cells, 6 feet (1.8 m) of DNA gets crammed into chromosomes that fit inside a 6-µm-wide nucleus. The proteins that help pack up that genetic material are histones, which act as spools around which DNA coils. These proteins don’t just play a structural role. Through processes that unwind and re-wind these coils of DNA, histones help regulate which genes are expressed at a given time.

Now, a new study reports that these proteins also have another, more ancient gig. They can act as enzymes that reduce copper ions—which cells need for metabolic processes—from a toxic form, Cu(II), to a usable one, Cu(I). This enzymatic role may have allowed single-cell organisms to cope with a huge rise in oxygen levels on Earth. It may also have had a hand in the evolution of more complex cells, called eukaryotes, that later came became multicellular organisms.

“Our work suggests that the presence of histones was actually essential for the formation of the first eukaryotes,” says Siavash Kurdistani, a biochemist at the University of California, Los Angeles who led the study.

Scientists think that the earliest living cells used metal ions to power their biochemistry. But the sharp increase in oxygen on the planet a little over 2 billion years ago—which geologists refer to as the Great Oxidation Event—made a lot of these metals unusable because the high levels of oxygen converted them to forms that were toxic to the cells.

The histones that we carry in our eukaryotic cells descend from similar but simpler proteins in a class of ancient one-celled organisms called archaea, which existed during that oxygen jump. Unlike eukaryotes, these organisms have small genomes, and they don’t have a nucleus, suggesting that the cells didn’t need histones’ DNA-packing abilities. So Kurdistani wondered whether these ancient histones might have originally played a different role and whether that role is conserved in histones today.

Histone proteins that are present in both archaea and eukaryotes consist of a tetramer of two H3 and two H4 proteins. A decades-old study hinted that two pairs of the amino acids cysteine and histidine, located at the point where the two H3 proteins meet, might bind metal ions. Based on that study, and what Kurdistani calls a “wild guess,” he and his colleagues set out to probe whether these proteins could act as enzymes to reduce copper.

They conducted two sets of experiments. First, they mutated the amino acid sequence of a histone protein in a simple eukaryote, Saccharomyces cerevisiae, at the region where metal-binding activity had been suggested. The eukaryotic cells containing the mutant histones had lower levels of Cu(I) ions, suggesting that the histone was indeed involved in reducing copper. In another experiment, they determined that the human H3-H4 tetramer could reduce copper at a decent rate in a test tube (Science 2020, DOI: 10.1126/science.aba8740).

“They’ve shown that in isolation, [human histones] are actually quite respectable enzymes,” says Karolyn Luger, a biochemist who studies the structures of DNA and histones at the University of Colorado Boulder and was not involved in the study but did write an accompanying commentary about it. Today’s eukaryotic cells have evolved multiple other ways of keeping copper in its non-toxic Cu(I) form, but the fact that histones still seem to do so strongly suggests that it might have been their original job, she says.

“This is a big story,” says Steven Henikoff, a biologist who studies histones at the Fred Hutchinson Cancer Research Center and who was not involved in the study. Around the time of the Great Oxidation Event, eukaryotic cells also started to host mitochondria, cellular compartments that act as metabolic power sources. The fact that Cu(I) is key to mitochondrial function might mean that histones play a previously unrecognized role in cell metabolism, he says.

Indeed, Kurdistani and his colleagues are now exploring the role of histones in mitochondrial diseases.

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