The new gene family helps control carbon dioxide fixation, which is the first step towards making high-energy molecules that feed the planet's organisms.
Various ways of affecting light-capturing antennae can cause cyanobacteria to either remain content or become stressed. The different responses depend on the species and the nature of the modification.
The HCP2 protein is an ancestor of proteins that are known to protect against damage caused by excess light exposure. The study is the first of its kind to structurally and biophysically analyze a protein from the recently discovered HCP family.
These ancient proteins will both add to our knowledge of the evolution of photosynthesis and open exciting doors to applications in fields like medicine and biotechnology.
Her poster showcased a newly discovered family of light-sensitive proteins of interest for renewable energy and medical applications.
The Kerfeld lab has analyzed over 200 sets of cyanobacteria DNA. This knowledge is getting us closer to understanding how to build synthetic factories that will someday produce green fuels or products used to diagnose diseases.
Scientists are learning how bacterial nanofactories are constructed in nature. Recent experiments show we could engineer their building blocks into new structures, for useful applications.
Turning the evolutionary clock back on a light-sensitive protein
We are inching closer to the day where we can use light to help cure diseases. The key is harnessing the power of proteins that are sensitive to light.
The OCP and its homologs, protect cyanobacteria when they are exposed to too much sunlight, which would otherwise damage the photosynthetic systems, and if extreme, damages the cell itself.
And just as shining light triggers the OCPs activity, scientists want to use that response to activate engineered, custom health technologies (jump to section).
But first, we need to understand how OCP and its relatives work, according to Sigal Lechno-Yossef, a post-doc in the Kerfeld lab.
In her latest study, published in The Plant Journal, Sigal shows how the two parts of the OCP interact when split apart. She also manages to create new, synthetic OCPs by mixing and matching the building blocks from different types of the OCP found in nature.
In nature, proteins are made up from a limited number of domains – think of them as Lego blocks – that combine in different ways.
The OCP is made out of two blocks, called C-terminal domain and N-terminal domain, spanned by a carotenoid pigment that bolts the two parts together.
This is how they work (see both caption and gif):
Sigal and her colleagues in the Kerfeld Lab suspect that the OCP, as we know it today, is the result of ancestors of the two domains joining together, millions of years ago. In evolution, genes for proteins that work collaboratively sometimes become permanently fused into a single, larger protein.
Sigal reversed this evolutionary event in the lab – call it devolution. “We wanted to better understand the evolution process of the OCP from domain homologs found in cyanobacteria today,” Sigal says.
The scientists broke down the connecting carotenoid bond to split apart an OCP protein. Then, they put both domains into a test host to see if they would find each other and connect again – basically retracing what they think was the evolutionary process.
“Without carotenoid, the two parts stayed separate. Once we put in the carotenoid, they latched onto each other. We basically created multiple synthetic versions of the OCP!”
The synthetic OCP reactions were similar to their natural cousins' in the presence of light. But for some reason, probably in the fine details of their structures, only one of the synthetic versions came back together in the dark.
As a bonus, even though the two OCP domains remained separate without the carotenoid bolt, that configuration yielded some interesting insights.
“In the OCP, the N-terminal domain binds to the carotenoid more strongly,” Sigal says. “When we isolated the domains, we found that, the C-terminal domain, when on its own, can bind to the carotenoid.”
Proteins similar to the C-terminal domain are widespread in plants, bacteria, and some animals, which opens new possibilities to explore engineering applications in a range of organisms, beyond bacteria.
Cheryl Kerfeld, principal investigator at the Kerfeld lab, thinks that precise knowledge of the structures of the various OCP building blocks makes them especially amenable to engineering.
The long-term goal is to use the OCP and its separate subcomponents in new, synthetic systems, specifically optogenics, a recently developed technique that uses light to control processes in living cells.
See how shining light controls a fly's escape response, in the video below.
Optogenetics, highlighted in a 2010 Science article on Breakthroughs of the Decade," is showing us how the brain works, how we learn, or how we wake up. Scientists hope that targeting specific brain cells will help us cure Parkinson’s or Alzheimer’s, even combat mental illnesses.
Light-sensitive proteins, similar to the OCP, are key to activating and controlling events in optogenetic applications. Although OCP has yet to be tried in a specific optogenetic application, the Kerfeld Lab thinks their properties make them likely to be useful.
“OCPs respond faster to light, compared to the current light-sensitive proteins used in optogenetic experiments,” Sigal says. “They are also so flexible in how they break apart and come back together. They are a great candidate.”
She adds, “Now that we’ve shown we can make artificial hybrid OCPs, we have a wider range of options." For example, if a patient requires multiple doses of medicine, their intake could be controlled with a synthetic OCP that assembles and disassembles to control dosages.
Or, OCP domains could be used separately, for example, as a kill switch for treatments that require single doses, as opposed to multiple cycles.
“We are still in the theoretical phase of imagining applications, but we are not far from where we can start experimenting with synthetic systems.”
This work was primarily funded by the US Department of Energy, Office of Basic Energy Sciences.
The protein, peroxiredoxin Q, is known to maintain a healthy balance of chemicals and energy levels in chloroplasts. The new research shows the protein also impacts the system that produces chloroplast membranes.
The CAMTA system - which is known to protect plants from cold weather - plays a newly discovered role: when bacteria invade a leaf, CAMTA warns neighboring, unaffected leaves to prepare for invasion.
When algae get stressed, they hibernate and store energy in forms that we can use to make biofuels. Understanding how stress impacts algal hibernation could help scientists lower the cost of biofuels production.