by Fred Neidhardt
The following is a personal account of the beginning years of what is now called proteomics. Odd that I, almost a Luddite, should be writing about the origin of a field initiated by a dramatic technical advance; I tend to avoid complex new scientific instruments and techniques. As a graduate student under Boris Magasanik at Harvard Medical School during the early 1950s, I was glad that my project (induced enzyme synthesis in bacteria) could readily be approached with simple technology. Bacterial growth could be monitored turbidimetrically with a Klett colorimeter; the same instrument could provide colorimetric assays of enzyme activities. Only the phage geneticists of that era, using sterile toothpicks to pick viral recombinants or mutants from plaques on Petri dishes, had it technologically easier.
Around me at that time in Harvard University’s Department of Bacteriology and Immunology (now Microbiology and Molecular Genetics) were gifted individuals who on occasion were forced to purify proteins using laborious and personally onerous techniques. Not a life for me, I decided, even though H. Edwin Umbarger assured me that purifying an enzyme “developed character.”
Beside laziness, there was a second, more fundamental, reason I never purified a protein. Cell growth was the biological event that had hooked me as a graduate student, and work that began by smashing cells into little bits seemed inappropriate.Nevertheless, within the next six years I would find myself absorbed in two major aspects of cell growth physiology that involved proteins, and these subjects would prove more intractable than the purification of proteins. Catabolite repression (or, more generally, how bacterial cells choose to utilize multiple carbon sources), and growth rate modulation (how bacterial cell size and composition are interrelated with growth rate) were two processes directly related to cell growth rate.