Role of glucose-6-phosphate in the regulation of aspartate semialdehyde dehydrogen ase in Escherichia coli

Boy, E

doi:10.1016/0378-1097(79)90014-4

Cited by 1 publication

(3 citation statements)

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“…Ampicillin (50 itg/ml) was added to the growth medium of plasnid harboring strains. growth represses ASA-dehydrogenase activity (compare lines 2 and 1); (iii) lysine limitation (obtained after growth in the chemostat of strain RM 4104, an auxotrophic Lys-mutant) leads to derepression of ASA-dehydrogenase activity (compare lines 3 and 2); (iv) multivalent regulation by threonine and methionine-induced limitation of growth is also observed with strain 106 G61 in the presence of 10 mM L-lysine, conditions known to lead to a decreased threonine and methionine pool (Boy and Patte, 1972; compare lines 4 and 2); and (v) accumulation of glucose-6-phosphate (strain G21M1, apgi mutant grown in fructose + glucose medium; Boy and Patte, 1979) also represses ASA-dehydrogenase to a greater extent (compare lines 6 and 2). The regulatory pattem of the asd gene in the plasmid is thus very similar to that of the chromosomal gene.…”

Section: Isolation and Purification Of The Asd Genementioning

confidence: 86%

“…gLysine was added at 10 mM and bacteria were taken after 16 h of growth; see Boy and Patte (1972). h and i: G21 MI was grown in repression conditions, either in 0.40o fructoseh or in 0.4%o fructose + 0.4% glucose'; in the latter conditions glucose-6 phosphate accumulation occurs in pgi strains; see Boy and Patte (1979).…”

Section: Isolation and Purification Of The Asd Genementioning

confidence: 99%

“…The asd gene encodes aspartic semialdehyde dehydrogenase (ASA-dehydrogenase; EC 1.2.1.11). This gene is interesting for several reasons: (i) it belongs to the common part of the biosynthetic pathways of lysine, threonine, and methionine (Theze et al, 1974); (ii) its synthesis is multivalently repressed by these amino acids, the efficiency of derepression being greatest in the case of lysine limitation (Boy and Patte, 1972); (iii) a regulatory (and unexplained) role of glucose-6-phosphate has also been described, possibly at the transcriptional level (Boy and Patte, 1979); (iv) the allelic state of the relA gene modifies the expression of the gene (Patte et al, 1980); and (v) the protein has been purified; it is a dimer composed of identical protomers of mol. wt.…”

Section: Introductionmentioning

confidence: 99%

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Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal.

Haziza¹,

Stragier²,

Patte³

1982

The EMBO Journal

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The asd gene of escherichia coli encodes aspartic semialdehyde dehydrogenase, an enzyme involved in lysine, threonine, and methionine biosynthesis; its synthesis is controlled by a multivalent repression mechanism. It was cloned in plasmid pBR322 and its complete nucleotide sequence determined. The sequence predicts a polypeptide chain of 367 amino acids, in good agreement with results obtained for the purified protein (Biellmann et al., 1980a). Our data indicate a Cys residue instead of a His residue, which was proposed after covalent labeling of the active center of the enzyme; this is more in line with the catalytic site of glyceraldehyde‐3‐phosphate dehydrogenase, an enzyme which carries out a similar reaction. The nucleotide sequence that precedes the translational start does not display any of the characteristic features of an attenuation signal. Hence the expression of the asd gene is probably not controlled in the same way as other multivalently repressed operons such as ilva and thr.

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Section: Isolation and Purification Of The Asd Genementioning

confidence: 86%

Section: Isolation and Purification Of The Asd Genementioning

confidence: 99%