University of Wollongong researchers have played their part in revealing the inner workings of pathogenic bacteria.
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This breakthrough will aid in the fight against deadly bacteria and help to develop new cures.
An Australian, Czech Republic and an international team comprising German, US and Finnish researchers used some of the world's most powerful microscopes to discover a unique molecular mechanism that allows pathogenic bacteria to maintain efficient gene expression.
The new insights are published in back-to-back articles in Nature Communications, a leading scientific journal. The Australian team is headed by Dr Gkhan Tolun from UOW and Professor Peter Lewis from the University of Newcastle.
They studied the HelD complex of RNAP from an important model bacterium, Bacillus subtilis, closely related to dangerous human pathogens such as Bacillus anthracis (anthrax) and Clostridium difficile (lethal pseudomembranous colitis and diarrhea).
RNAP reads the genetic code in our DNA and transcribes it into another molecule called RNA that carries out other vital functions, such as producing the proteins that keep us alive.
"In our fight against such deadly bacteria, structural biology is one of the most powerful weapons we have," Dr Tolun said.
"Once we see the structures of these bio-nano-machines, we can better understand how they work - structure dictates function! Understanding how such vital biological processes work then leads to designing means of interfering with them.
"That means we can use the molecular structures we determine to develop drugs that bind to these essential molecular machines and inhibit their functions, resulting in the death of that bacterial cell. Ultimately, it allows us to develop novel cures that currently do not exist!"
The Australian team's paper is the first high-impact paper with a significant contribution from UOW researchers to come out of UOW's new $80-million Molecular Horizons Cryo-EM facility.
Both of the high-resolution cryo-EM structures of the RNAP macromolecular complexes reported in this paper have been determined at UOW.
"We have a world-class Cryo-EM facility here at UOW that allows us to take very high-resolution pictures of individual molecular machines," Dr Tolun said.
"These images are much like when you get an X-ray, but of the tiny biological machines instead of your body. Then, we use supercomputers to process these images to reconstruct the three dimensional atomic structure of these assemblies."
In the other papers published in Nature Communications, the Czech consortium discovered a variant of the same mechanism in Mycobacteria, the causative agents of tuberculosis and other devastating diseases.
The consortium of researchers from Germany, the USA and Finland elucidated how a particular auxiliary component of RNAP helps HelD in its action in some bacteria.
These three publications put together reveal a previously unknown mechanism for RNAP rescue and recycling in these bacteria, leading the way to developing novel therapeutics against them.
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Agron Latifi
Wollongong born and bred. I love reporting about the Illawarra region and have been doing it for more than 20 years. I've moved into sport recently after covering the education round for the last five plus years for the Illawarra Mercury. It's been a great pleasure.
Wollongong born and bred. I love reporting about the Illawarra region and have been doing it for more than 20 years. I've moved into sport recently after covering the education round for the last five plus years for the Illawarra Mercury. It's been a great pleasure.
