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When E. coli Bl21(DE3), a strain that did not express additional rare tRNAs, was transformed with the cloned T. acidophilum ATPase A subunit, no additional protein bands were observed in extracts of induced cells (not shown).
unknown, but it may have a role in cell division [ 11 ] . RNase P, which consists of the protein subunit RnpA and a catalytic RNA subunit, is essential for generating mature tRNAs by cleaving the 5'-terminal leader sequences of precursor tRNAs [ 16 ] . rpmH encodes ribosomal protein L34, and DnaA is the initiator protein for chromosome replication.
Based on the normal function of GCN2-like proteins [ 25 ] , these findings suggest that uncharged tRNAs are more prevalent within the cells during this time relative to either growing cells or to cells immediately after removal of the food source.
In yeast and mammalian cells, GCN2 is a protein that senses amino acid starvation and brings about altered cell physiology in response to such starvation [ 24 25 ] . GCN2 is a protein kinase that phosphorylates the α subunit of the translation initiation factor eIF2 [ 26 ] . The GCN2 protein from yeasts, Drosophila , and mammals is composed of three domains: a pseudokinase domain that may function as a regulatory domain, a kinase domain, and a HisRS domain that shares significant similarity to histidyl-tRNA synthetases [ 27 28 29 30 ] . Studies of yeast GCN2 revealed that the HisRS domain binds uncharged tRNAs that accumulate when cells are starved for amino acids [ 31 32 ] . As a result the kinase domain is activated and phosphorylates eIF2α at Ser51.
E. coli has 86 tRNAs, and most of these appear to be present in the ancestor (the parsimony criterion for presence of a tRNA in the ancestor, based on distribution in sequenced genomes, is somewhat unreliable because of sequence homology among different tRNA genes).
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