Proteins Interacting With RNA And DNA Are Surprisingly Similar

faster than they ordinarily would because the rate of protein production is doubled.

An antibiotic called thiostrepton works by attaching to both the L11 protein and the ribosomal RNA of infection-causing bacteria, preventing the production of protein and controlling the bacterial infection.

But, although a nearly identical protein also is attached to the ribosomes of higher forms of life, the antibiotic will only bind to the bacterial RNA.

How the antibiotic distinguishes between the two types of RNA is a mystery, since the segment of RNA that the protein binds to is very similar in bacteria and higher organisms. There must be specific features that are only present in the bacterial RNA, Draper said.

"Those are very handy features because that means you can design drugs to target just bacteria and not kill the host," he said.

RNA, or ribonucleic acid, is essential in the manufacture of proteins ranging from vital enzymes and hormones to hemoglobin and structural components. DNA, or deoxyribonucleic acid, contains the huge library of genetic information organisms need to reproduce and to make RNA. Both RNA and DNA are made of molecules called nucleotides. But RNA is a single-stranded compound of the molecules and DNA has two strands, which are connected in a twisting structure called a double helix.

Learning why the RNA- and DNA-binding proteins are so similar could lead to insights specifically about the protein's interaction with RNA, which could shed light on how the antibiotic distinguishes between the two forms of RNA. Such insights could one day enable scientists to make better antibiotics.

In the search for more effective antibiotics, Draper is working with a biotechnology company to investigate compounds that bind to the same segment of RNA as thiostrepton. Thiostrepton is not water-soluble enough to be taken orally. Consequently, the antibiotic, which is used to treat ear infections in animals, can be administered only externally, as a

Contact: Emil Venere
Johns Hopkins University

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