The Kerfeld lab has analyzed over 200 sets of cyanobacteria DNA, towards someday building synthetic factories that will produce green fuels or medical diagnostic products.
'Hoarding' resources in the same location encourages more efficient chemical reactions. Someday, we could use this system to enhance the production of rubber, biofuels, and other commodities.
The genetically engineered shell is based on natural structures and the principles of protein evolution. Scientists see such structures as a source of new industrial or medical technologies.
MSU scientists report how cyanobacteria line up their CO2-fixing factories within them in a system that works like Velcro. The research is part of an effort to control and repurpose these factories to make products for human consumption.
The new methods let scientists assemble the factories on demand and insert custom molecules inside them for further processing. The aim is to eventually design sustainable medical, industrial, or energy applications.
The Kerfeld lab announces two new methods for manipulating bacterial factories for biotech aims: one is to screen and extract the factories, the other is to predictably insert custom enzymes in them.
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.
The new compartment, widely spread among different kinds of bacteria, might be reassembled to someday sustainably produce “green” chemicals, medicines, and renewable energy.
In a new Science publication, The Kerfeld lab show us the details of bacterial organelle shells for the first time ever, making it easier to target them for medical or renewable energy applications.
How to build artificial nanofactories to power our futures: Logistics
When we buy a new phone or laptop online, we assume it will be delivered to our doorstep in a matter of days.
But we mostly miss the complex logistics that make this happen: ships, planes, trains, and trucks that move products, starting from raw materials in mines, to factories for assembly, to warehouses for storage, and up to our doorsteps.
Scientists at the MSU-DOE Plant Research Laboratory are trying to build artificial nanofactories to sustainably produce industrial materials or medical tools.
And like with getting new phones, these artificial nanofactories of the future will need an army of "nano" vehicles to deliver valuable chemical products.
But we don’t know enough about the logistics just yet.
It turns out bacteria in nature have the blueprint for us to copy. They house nanofactories, called bacterial microcompartments (BMCs) - that fill many purposes, depending on the host.
In cyanobacteria, for example, BMCs build useful compounds from carbon dioxide pulled from the atmosphere. Or, some pathogenic bacteria use them to outcompete “good” bacteria.
In a new study, published in the journal Biochemistry, Jeff Plegaria and the Kerfeld lab reveal the structure and function of a widespread BMC protein that contributes to the logistics of creating products, taking us closer to repurposing BMCs for our own uses.
Describing the Fld1C flavoprotein
Jeff and his colleagues noticed that many natural BMCs – especially a type that degrades carbon to help make useful energy compounds – contain genes for flavoproteins right next to the primary genes responsible for constructing and operating the BMCs.
Primary genes include instructions for building and managing BMCs, transporting materials back and forth, and so on.
And being close to the core genes meant flavoproteins play an important role within BMCs.
So, what do flavoproteins do?
“They are electron transfer proteins found in many bacteria and other biological pathways in nature. Electron transfer, or flow, is a fundamental process in nature,” Jeff says.
“Understanding electron flow in BMCs is crucial, because it is part of the assembly line that leads to the creation of final chemical products. But, we still don’t know much about how flavoproteins work in BMCs.”
In the study, Jeff zoomed in on one BMC flavoprotein, which his group named Fld1C.
They were able to characterize it, revealing its structure, describing its physical features, and confirming its ability to take part in electron transfer reactions.
“With help from scientists at Argonne National Laboratory, we generated an agent that can pass an electron on to a willing acceptor. We successfully showed our Fld1C flavoprotein accepting an electron from that agent.”
“Understanding these logistics – how electrons flow in and out of BMCs – is vital to building and controlling synthetic BMCs for custom applications.”
Such applications could include producing industrial materials like rubber or petroleum, without relying on fossil fuels.
Or we could build medical tools that disarm BMCs in “bad” bacteria – like Salmonella – and prevent them from wreaking their havoc.
This work was primarily funded by the US Department of Energy, Office of Basic Energy Sciences. The authors would also like to thank Dr. Michaela TerAvest for helping characterize the flavoprotein redox properties and the Argonne National Laboratory for help with confirming electron transfer reactions.
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.