Editing Sidney Altman (section)

==Career==
After receiving his Ph.D., Altman embarked upon the first of two research fellowships. He joined [[Matthew Meselson]]'s laboratory at [[Harvard University]] to study a DNA [[endonuclease]] involved in the replication and recombination of T4 DNA. Later, at the [[Medical Research Council (UK)|MRC]] [[Laboratory of Molecular Biology]] in Cambridge, England, Altman started the work that led to the discovery of [[RNase P]] and the enzymatic properties of the RNA subunit of that ribozyme. [[John Derek Smith|John D. Smith]], as well as several postdoctoral colleagues, provided Altman with very good advice that enabled him to test his ideas. "The discovery of the first radiochemically pure precursor to a [[Transfer RNA|tRNA]] molecule enabled me to get a job as an assistant professor at Yale University in 1971, a difficult time to get any job at all".<ref name=r1/>

Altman's career at Yale followed a standard academic pattern with promotion through the ranks until he became Professor in 1980. He was Chairman of his department from 1983 to 1985 and in 1985 became the Dean of Yale College for four years. On July 1, 1989, he returned to the post of Professor on a full-time basis. His doctoral students include [[Benjamin C. Stark|Ben Stark]].

While at Yale, Altman's Nobel Prize work came with the analysis of the catalytic properties of the [[ribozyme]] [[RNase P]], a [[ribonucleoprotein]] particle consisting of both a structural RNA molecule and one (in [[prokaryotes]]) or more (in [[eukaryotes]]) proteins. Originally, it was believed that, in the bacterial RNase P complex, the protein subunit was responsible for the catalytic activity of the complex, which is involved in the maturation of tRNAs. During experiments in which the complex was reconstituted in test tubes, Altman and his group discovered that the RNA component, in isolation, was sufficient for the observed catalytic activity of the [[enzyme]], indicating that the RNA itself had catalytic properties, which was the discovery that earned him the Nobel Prize.<ref name=BBY1990/> Although the RNase P complex also exists in eukaryotic organisms, his later work revealed that in those organisms, the protein subunits of the complex are essential to the catalytic activity, in contrast to the bacterial RNase P.