COLUMBUS , Ohio A new understanding of an enzyme important for the transfer of genetic information in bacteria may help scientists improve current antibiotics and also create antibiotics that are less vulnerable to resistance.
Researchers used extremely powerful imaging techniques to see, for the first time, exactly what happens between bacteria and antibiotics at the atomic level. They report their findings in two studies in the journal Nature.
The work provides the most detailed view yet of an enzyme structure that is key to turning on the genes that make bacteria work, said Irina Artsimovitch, a co-author on both studies and an associate professor of microbiology at Ohio State University.
Artsimovitch worked with Dmitry Vassylyev, the lead author of both studies and a professor of biochemistry and molecular biology at the University of Alabama at Birmingham. The two conducted the study with researchers from the University of Alabama at Birmingham , the University of Wisconsin-Madison and the University of Nebraska Medical Center.
In the first study, the team found that they could create a detailed image of the elongation complex, a structure formed by RNA polymerase. RNA polymerase is the enzyme responsible for setting gene expression in motion, a process called transcription. Without a properly functioning RNA polymerase, a cell will die.
RNA polymerase spends most of its working hours as the elongation complex, Artsimovitch said. The complex makes RNA's messages one step at a time, many thousands of times, until its completion.
This structure is important from a physiological point of view, not only for antibiotic design, but also because faults in the complex have been implicated in many diseases such as hereditary cancers.
Artsimovitch and her colleagues used the bacterium Thermus thermophilus to run their experiments. While T. thermophilus won't make a human sick, the bacterium is wide
Contact: Irina Artsimovitch
Ohio State University