Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase

Goncharoff, Paul; Nichols, Brian P.

doi:10.1128/jb.159.1.57-62.1984

Cited by 66 publications

(21 citation statements)

References 28 publications

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“…The predicted amino acid sequences of ASAl and ASA2 proteins were fit to the alignment of bacterial and yeast AS a subunit sequences (Crawford, 1989), with minor modifications. Nichols, 1984), the a subunit of PABA synthase. The TRP2 sequence was modified by the introduction of frameshifts at amino acid positions 622 and 638, as described by Crawford (1989).…”

Section: Asa7 and Asa2 Encode Functional As A Subunitsmentioning

confidence: 99%

“…Recent studies of AS from Salmonella typhimurium (Caligiuri and Bauerle, 1991) and Brevibacferium lacfofermenfum (Matsui et al, 1987) have pinpointed particular amino acids in the a subunit that are important for feedback inhibition by tryptophan. Microbial AS genes have homology to genes encoding at least two other chorismate-utilizing enzymes, para-aminobenzoic acid (PABA) synthase (Goncharoff and Nichols, 1984;Crawford, 1989) and isochorismate synthase (Ozenberger et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

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Two Anthranilate Synthase Genes in Arabidopsis: Defense-Related Regulation of the Tryptophan Pathway

Niyogi¹,

Fink²

1992

The Plant Cell

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Arabidopsis thaliana has two genes, ASA1 and ASA2, encoding the alpha subunit of anthranilate synthase, the enzyme catalyzing the first reaction in the tryptophan biosynthetic pathway. As a branchpoint enzyme in aromatic amino acid biosynthesis, anthranilate synthase has an important regulatory role. The sequences of the plant genes are homologous to their microbial counterparts. Both predicted proteins have putative chloroplast transit peptides at their amino termini and conserved amino acids involved in feedback inhibition by tryptophan. ASA1 and ASA2 cDNAs complement anthranilate synthase alpha subunit mutations in the yeast Saccharomyces cerevisiae and in Escherichia coli, confirming that both genes encode functional anthranilate synthase proteins. The distributions of ASA1 and ASA2 mRNAs in various parts of Arabidopsis plants are overlapping but nonidentical, and ASA1 mRNA is approximately 10 times more abundant in whole plants. Whereas ASA2 is expressed at a constitutive basal level, ASA1 is induced by wounding and bacterial pathogen infiltration, suggesting a novel role for ASA1 in the production of tryptophan pathway metabolites as part of an Arabidopsis defense response. Regulation of key steps in aromatic amino acid biosynthesis in Arabidopsis appears to involve differential expression of duplicated genes.

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Section: Asa7 and Asa2 Encode Functional As A Subunitsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Two Anthranilate Synthase Genes in Arabidopsis: Defense-Related Regulation of the Tryptophan Pathway

Niyogi¹,

Fink²

1992

The Plant Cell

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“…2); homologous regions are particularly obvious in the carboxy termini of the proteins. (Goncharoff and Nichols [14] have noted the relatedness between pabB and trpE at the amino acid and nucleotide level.) The trpE and pabB genes both show similarities of 53% with entC.…”

Section: Resultsmentioning

confidence: 99%

An Escherichia coli enterobactin cluster gene with sequence homology to trpE and pabB

Elkins¹

1988

FEMS Microbiology Letters

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An Escherichia coli gene located in the enterobactin gene cluster between fepB and entE was sequenced. The nucleotide sequence showed a 53% similarity to those of the related genes pabB and trpE; at the amino acid level, the homology was approximately 20%. The pabB and trpE genes encode enzymes that use chorismate as a substrate suggesting that the gene sequenced here is entC,. whose cognate protein is isochorismate synthase. A binding site for the iron regulatory protein Fur was found upstream from entC and only 9 bp separated entC from entE, indicating that entCE are cotranscribed.

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“…Using SMX resistance as an indicator of the gene, a combination of subcloning, unidirectional deletions, and restriction enzyme site fill-ins and recircularization was used to narrow down the fragment generating SMX resistance to a 2800 bp BglII-PvuII fragment (see Figure 1). (Goncharoff and Nichols, 1984; Kaplan and Nichols, 1983).…”

Section: Isolation Of Paba Synthase Genementioning

confidence: 99%

Para‐aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme

Edman

Goldstein

Erbe

1993

Yeast

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The Saccharomyces cerevisiae gene for para-aminobenzoate (PABA) synthase has been identified based upon its ability to confer sulfonamide resistance when present on a multicopy episomal vector. The 3840 bp DNA sequence fragment reported here contains a 2199 bp open reading frame encoding a 733 amino acid protein with similarity to the two components of PABA synthase described for prokaryotes (Escherichia coli PabA and PabB), suggesting that PABA synthase is bifunctional in yeast. The cloned sequence was confirmed to be PABA synthase by gene disruption. Chromosome gel analysis places the gene for PABA synthase on chromosome XIV.

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Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase

Cited by 66 publications

References 28 publications

Two Anthranilate Synthase Genes in Arabidopsis: Defense-Related Regulation of the Tryptophan Pathway

Two Anthranilate Synthase Genes in Arabidopsis: Defense-Related Regulation of the Tryptophan Pathway

An Escherichia coli enterobactin cluster gene with sequence homology to trpE and pabB

Para‐aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme

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