Gl. Matters et Si. Beale, BIOSYNTHESIS OF DELTA-AMINOLEVULINIC-ACID FROM GLUTAMATE BY SULFOLOBUS-SOLFATARICUS, Archives of microbiology, 161(3), 1994, pp. 272-276
The extremely thermophilic, obligately aerobic bacterium Sulfolobus so
lfataricus forms the tetrapyrrole precursor, delta-aminolevulinic acid
(ALA), from glutamate by the tRNA-dependent five-carbon pathway. This
pathway has been previously shown to occur in plants, algae, and most
prokaryotes with the exception of the a-group of proteobacteria (purp
le bacteria). An alternative mode of ALA formation by condensation of
glycine and succinyl-CoA occurs in animals, yeasts, fungi, and the alp
ha-proteobacteria. Sulfolobus and several other thermophilic, sulfur-d
ependent bacteria, have been variously placed within a subgroup of arc
haea (archaebacteria) named crenarchaeotes, or have been proposed to c
omprise a distinct prokaryotic group designated eocytes. On the basis
of ribosomal structure and certain other criteria, eocytes have been p
roposed as predecessors of the nuclear-cytoplasmic descent line of euk
aryotes. Because aplastidic eukaryotes differ from most prokaryotes in
their mode of ALA formation, and in view of the proposed affiliation
of eocytes to eukaryotes, it was of interest to determine how eocytes
form ALA. Sulfolobus extracts were able to incorporate label from [I-C
-14]glutamate, but not from [12-C-14]glycine, into ALA. Glutamate inco
rporation was abolished by preincubation of the extract with RNase. Su
lfolobus extracts contained glutamate-l-semialdehyde aminotransferase
activity, which is indicative of the five-carbon pathway. Growth of Su
lfolobus was inhibited by gabaculine, a mechanism-based inhibitor of g
lutamate-1-semialdehyde aminotransferase, an enzyme of the five-carbon
ALA biosynthetic pathway. These results indicate that Sulfolobus uses
the five-carbon pathway for ALA formation.d