Abstract
When stringent cells of Escherichi coli are starved for an amino acid, a guanine nucleotide derivative, MS1 , identified as ppGpp [l] , rapidly accumulates to relative high concentrations [2, 31 . The level of this derivative usually exceeds that of guanosine triphosphate [3,4], GTP (pppG), which in turn is in excess over guanosine diphosphate, GDP (ppG) [5]. In general, the level of MS1 can be directly correlated with the rate of cell growth [6] . We show here that MS1 can inhibit a step in protein synthesis; specifically the formation of the initiation complex containing formylmethionyltRNAf, 70 S ribosomes and messenger RNA.
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