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Title: Expression of the Synechocystis sp. strain PCC 6803 tRNA sup Glu gene provides tRNA for protein and chlorophyll biosynthesis

Journal Article · · Journal of Bacteriology; (USA)
OSTI ID:5926187
;  [1]
  1. Yale Univ., New Haven, CT (USA)

In the cyanobacterium Synechocystis sp. strain PCC 6803 (Synechocystis 6803) {delta}-aminolevulinic acid (ALA), the sole precursor for the synthesis of the porphyrin rings of heme and chlorophyll, is formed from glutamate activated by acylation to tRNA{sup Glu}. We report here that Synechocystis 6803 possesses a single tRNA{sup Glu} gene which was transcribed as monomeric precursor tRNA and matured into the two tRNA{sup Glu} species. They differed in the extent of modification of the first anticodon base, 5-methylaminomethyl-2-thiouridine. The two tRNA species had equivalent capacities to stimulate the tRNA-dependent formation of ALA in Synechocystis 6803 and to provide glutamate for protein biosynthesis in an Escherichia coli-derived translation system. These results are in support of a dual role of tRNA{sup Glu}. The levels of tRNA{sup Glu} were examined by Northern (RNA) blot analysis of cellular RNA and by aminoacylation assays in cultures of Synechocystis 6803 in which the amount of chlorophyll synthesized was modulated over a 10-fold range by various illumination regimens or by the addition of inhibitors of chlorophyll and ALA biosynthesis. In these cultures, the level of tRNA{sup Glu} was always a constant fraction of the total tRNA population, suggesting that tRNA{sup Glu} and chlorophyll levels are regulated independently. In addition, the tRNA{sup Glu} was always fully aminoacylated in vivo.

OSTI ID:
5926187
Journal Information:
Journal of Bacteriology; (USA), Vol. 172:11; ISSN 0021-9193
Country of Publication:
United States
Language:
English