Albert Schatz streptomycin co-discoverer awarded with Rutgers medal

Albert Schatz – co-discoverer of streptomycin antibiotic

Article on Albert Schatz

Biography & Contributions

Albert Schatz was an American microbiologist and science educator born on February 02, 1920 – died on January 17, 2005. Schatz is best known as the discoverer of the antibiotic, streptomycin.

Schatz first isolated a series of threadlike bacteria known as actinomycetes. In 1994 he was awarded with Rutgers medal.

In the university's soil microbiology laboratory under the direction of Selman Waksman, Schatz volunteered to search for soil-born microorganisms that would kill or inhibit the growth of penicillin-resistant bacteria including tubercle bacillus, the bacterium that causes tuberculosis (TB) and several Gram-negative bacteria. He named the antibiotic derived from these bacteria streptomycin.

Dr. Schatz also initiated research which led to the discovery of Nystatin, an antibiotic which controls fungus and yeast infections, when he was working at the New York State Department of Health in Albany in 1946.


Streptomycin is an antibiotic / antimycobacterial drug, the first of a class of drugs called aminoglycosides to be discovered, and it was the first effective treatment for tuberculosis. It is derived from the actinobacterium Streptomyces griseus. Streptomycin is a bactericidal antibiotic. Streptomycin can be used clinically to treat tuberculosis in combination with other medications and susceptible strains which cause bacterial endocarditis. Streptomycin also is used as a pesticide, to combat the growth of bacteria, fungi, and algae.

Streptomycin controls bacterial and fungal diseases of certain fruit, vegetables, seed, and ornamental crops, and it controls algae in ornamental ponds and aquaria. Streptomycin, in combination with penicillin, is used in a standard antibiotic cocktail to prevent bacterial infection in cell culture. Streptomycin is a protein synthesis inhibitor. It binds to the small 16S rRNA of the 30S subunit of the bacterial ribosome, interfering with the binding of formyl-methionyl-tRNA to the 30S subunit.

As a consequence codon will be misread, which causes eventual inhibition of protein synthesis and ultimately death of microbial cells through mechanisms that are still not understood. Speculation on this mechanism indicates that the binding of the molecule to the 30S subunit interferes with 50S subunit association with the mRNA strand. This results in an unstable ribosomal-mRNA complex, leading to a frameshift mutation and defective protein synthesis; leading to cell death.

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