Thomas Cech

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Thomas Robert Cech (December 8, 1947 in Chicago) is a Nobel Laureate in chemistry.

He grew up in Iowa City, Iowa. In 1966, he entered Grinnell College where he obtained a B.A. in 1970. In 1975, Cech completed his Ph.D. in Chemistry at the University of California, Berkeley and in the same year, he entered the Massachusetts Institute of Technology in Cambridge where he engaged in postdoctoral research. In 1978, he obtained his first faculty position at the University of Colorado where he lectured undergraduate students in chemistry and biochemistry, and where he remains on the faculty, currently as Distinguished Professor in the Department of Chemistry and Biochemistry. In 2000, Dr. Cech succeeded Purnell Choppin as president of the Howard Hughes Medical Institute in Maryland. He also continues to head his world-renowned biochemistry laboratory in the University of Colorado, Boulder.

In December 2006 it was reported that he was among the candidates being considered for the presidency of Harvard University.[1]

[edit] Research Areas

Thomas Cech's main research area is that of the process of transcription in the nucleus of cells. He studies how the genetic code of DNA is transcribed into RNA. In the 1970s, Dr. Cech had been studying the splicing of RNA in the unicellular organism Tetrahymena thermophila when he discovered that an unprocessed RNA molecule could splice itself. In 1982, Dr. Cech became the first to show that RNA molecules are not restricted to being passive carriers of genetic information - they can have catalytic functions and can participate in cellular reactions. RNA-processing reactions and protein synthesis on ribosomes in particular are catalysed by RNA. RNA enzymes are known as ribozymes and have provided a new tool for gene technology. They also have the potential to provide new therapeutic agents - for example, they have the ability to destroy and cleave invading, viral RNAs.

Thomas Cech has a second, very different area of research - that of the structure and function of telomeres, the natural ends of linear chromosomes. He and his research group focus on the assembly, structure and function of telomerase, the enzyme that copies the telomeric sequences. The active site protein subunits of telomerase comprise a new class of reverse transcriptases, enzymes previously thought to be restricted to viruses and transposable elements. Telomerase is an important enzyme in biomedical terms due to the fact that it is activated in 90% of human cancers. Therefore, a drug that would inhibit its activity is much sought after as a cancer chemotherapeutic.