Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Researchers show fruit flies have latent bioluminescence

10.04.2014

New findings hold promise for expanded use of bioluminescence imaging tools

New research from scientists at the University of Massachusetts Medical School shows that fruit flies are secretly harboring the biochemistry needed to glow in the dark —otherwise known as bioluminescence.

The key to activating this latent ability is a novel synthetic analog of D-luciferin developed at UMMS. The findings, published in the journal Proceedings of the National Academy of Sciences, suggest that the inherent biochemistry needed for bioluminescence is more common than previously thought. Synthetic luciferins can unmask latent enzymatic activity capable of producing light in animals not known for their luminescence. This expands the scope of bioluminescence imaging for research, and adds new tools for the noninvasive studying of ongoing biological processes.

Few animals can naturally glow in the dark. The best known example, the firefly, creates bioluminescence when the small molecule D-luciferin is oxidized by the enzyme luciferase, which is only found in beetles.

... more about:
»bioluminescence »enzyme »reaction »synthetic

The luciferase enzyme is believed to have evolved from the fatty acyl-CoA synthetases (ACSLs) found in all insects. Both classes of enzymes are members of the adenylate-forming superfamily and can activate fatty acids. But only luciferase catalyzes light emission from D-luciferin. Stephen C Miller, PhD, associate professor of biochemistry and molecular pharmacology at UMass Medical School, had previously found that some mutations in the luciferase enzyme reduce light emission from the natural D-luciferin substrate, but improve light emission when using synthetic luciferins developed in his lab.

"This suggested to us that the failure of insect ACSLs to emit light with the beetle luciferase substrate D-luciferin didn't necessarily mean they weren't capable of the biochemistry needed to glow," said Dr. Miller, senior author of the PNAS study.

He hypothesized that ACSL enzymes in other insects are capable of a bioluminescent reaction similar to the firefly. The key was finding a small molecule to fill the role of D-luciferin, which is not a substrate for ACSLs, to kick start the biochemical reaction.

Suspecting that D-luciferin was in fact a poor substrate for ACSLs due to its shape, Miller and colleagues David Mofford, a fourth year doctoral candidate in the Graduate School of Biomedical Sciences and first author of the study and Randheer Gadarla, PhD, postdoctoral research fellow, tested a number of synthetic luciferins he had developed to see if they had the geometry necessary to initiate bioluminescence using the fatty acyl-CoA synthetase CG6178 found in the fruit fly Drosophila melanogaster.

Miller found that when this fruit fly protein was treated with a rigid synthetic analog of D-luciferin, named CycLuc2, it emitted a red glow. Simply adding CycLuc2 to live Drosophila cells was sufficient to make them glow as well. When CG6178 was expressed in mammalian cells, they too were able to emit light in the presence of CycLuc2.

"We think the unique rigid and asymmetric ring structure of the synthetic CycLuc2 molecule acts as a handle to help properly align it within the enzyme so adenylation can occur. Once that happens, the molecule can be oxidized to emit light," said Miller. "D-luciferin doesn't fit properly so the biochemical reaction necessary to initiate bioluminescence can't get started."

These findings suggest that other bioluminescent enzymatic activities may already exist in nature, waiting to be revealed by a suitable luciferin analog. Having multiple luciferases with unique substrates increases the amount of information that can be gained using this technique. And because it doesn't require changing the underlying DNA, utilizing endogenous proteins as luciferases could greatly impact the potential uses of bioluminescence imaging to study gene expression, understand infection, track cancer cells, or gauge the effectiveness of new drugs.

"These synthetic substrates expand the scope of bioluminescence beyond what was previously thought possible," said Miller. "It's going to give scientists new tools to study fundamental biological processes noninvasively in live cells and animals, possibly using an endogenous enzyme rather than firefly luciferase."

One of the next steps for Dr. Miller and colleagues will be exploring whether synthetic luciferins can unmask latent luciferase activity in human ACSL enzymes.

###

About the University of Massachusetts Medical School

The University of Massachusetts Medical School (UMMS), one of five campuses of the University system, comprises the School of Medicine, the Graduate School of Biomedical Sciences, the Graduate School of Nursing, a thriving research enterprise and an innovative public service initiative, Commonwealth Medicine. Its mission is to advance the health of the people of the Commonwealth through pioneering education, research, public service and health care delivery with its clinical partner, UMass Memorial Health Care. In doing so, it has built a reputation as a world-class research institution and as a leader in primary care education. The Medical School attracts more than $240 million annually in research funding, placing it among the top 50 medical schools in the nation. In 2006, UMMS's Craig C. Mello, PhD, Howard Hughes Medical Institute Investigator and the Blais University Chair in Molecular Medicine, was awarded the Nobel Prize in Physiology or Medicine, along with colleague Andrew Z. Fire, PhD, of Stanford University, for their discoveries related to RNA interference (RNAi). The 2013 opening of the Albert Sherman Center ushered in a new era of biomedical research and education on campus. Designed to maximize collaboration across fields, the Sherman Center is home to scientists pursuing novel research in emerging scientific fields with the goal of translating new discoveries into innovative therapies for human diseases.

Jim Fessenden | EurekAlert!
Further information:
http://www.umassmed.edu/

Further reports about: bioluminescence enzyme reaction synthetic

More articles from Life Sciences:

nachricht Antimicrobial substances identified in Komodo dragon blood
23.02.2017 | American Chemical Society

nachricht New Mechanisms of Gene Inactivation may prevent Aging and Cancer
23.02.2017 | Leibniz-Institut für Alternsforschung - Fritz-Lipmann-Institut e.V. (FLI)

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Breakthrough with a chain of gold atoms

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

Im Focus: DNA repair: a new letter in the cell alphabet

Results reveal how discoveries may be hidden in scientific “blind spots”

Cells need to repair damaged DNA in our genes to prevent the development of cancer and other diseases. Our cells therefore activate and send “repair-proteins”...

Im Focus: Dresdner scientists print tomorrow’s world

The Fraunhofer IWS Dresden and Technische Universität Dresden inaugurated their jointly operated Center for Additive Manufacturing Dresden (AMCD) with a festive ceremony on February 7, 2017. Scientists from various disciplines perform research on materials, additive manufacturing processes and innovative technologies, which build up components in a layer by layer process. This technology opens up new horizons for component design and combinations of functions. For example during fabrication, electrical conductors and sensors are already able to be additively manufactured into components. They provide information about stress conditions of a product during operation.

The 3D-printing technology, or additive manufacturing as it is often called, has long made the step out of scientific research laboratories into industrial...

Im Focus: Mimicking nature's cellular architectures via 3-D printing

Research offers new level of control over the structure of 3-D printed materials

Nature does amazing things with limited design materials. Grass, for example, can support its own weight, resist strong wind loads, and recover after being...

Im Focus: Three Magnetic States for Each Hole

Nanometer-scale magnetic perforated grids could create new possibilities for computing. Together with international colleagues, scientists from the Helmholtz Zentrum Dresden-Rossendorf (HZDR) have shown how a cobalt grid can be reliably programmed at room temperature. In addition they discovered that for every hole ("antidot") three magnetic states can be configured. The results have been published in the journal "Scientific Reports".

Physicist Dr. Rantej Bali from the HZDR, together with scientists from Singapore and Australia, designed a special grid structure in a thin layer of cobalt in...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Booth and panel discussion – The Lindau Nobel Laureate Meetings at the AAAS 2017 Annual Meeting

13.02.2017 | Event News

Complex Loading versus Hidden Reserves

10.02.2017 | Event News

International Conference on Crystal Growth in Freiburg

09.02.2017 | Event News

 
Latest News

From rocks in Colorado, evidence of a 'chaotic solar system'

23.02.2017 | Physics and Astronomy

'Quartz' crystals at the Earth's core power its magnetic field

23.02.2017 | Earth Sciences

Antimicrobial substances identified in Komodo dragon blood

23.02.2017 | Life Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>