Born in February 1937 in a small village in Extremadura, in southwestern Spain, Viñuela obtained his academic degrees at the University of Madrid before moving to the laboratory of Alberto Sols at the Spanish Research Council in Madrid. There he worked on carbohydrate metabolism, discovering the enzyme glucokinase, the synthesis of which depends on insulin and which is responsible for phosphorylation of glucose in the liver. He also demonstrated the allosteric properties of yeast phosphofructokinase, which has a regulatory binding site for ATP (the end-product of the pathway) that differs from the substrate site. The end-product inhibition of phosphofructokinase by ATP was proposed to act as a feedback control in the breakdown of glucose.
In 1964, Viñuela moved to New York University to work as a postdoctoral student in the laboratory of the Nobel prizewinner Severo Ochoa. At that time there was no molecular biology in Spain, so, to learn this relatively new area of biology, it was a must to move — preferably to the United States. This was a turning point in Viñuela's career. In New York he began collaborating with Charles Weissmann on research into the replication of bacteriophage MS2 RNA, especially the mechanism of parental-type ‘plus strand’ formation. This provided further insights into how MS2 RNA replicates. After this work he started to characterize the proteins induced after the infection of Escherichia coli with phage MS2, and to study translation of MS2 RNA. This was a time when the basic processes of the transfer of genetic information (replication, transcription and translation) started to be deciphered. The remarkable finding to emerge was that formyl methionine is the initiator of all the proteins encoded by the polycistronic MS2 RNA in E. coli, a result that quickly made its way into the textbooks.
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