Cloning of the Aspartase Gene (aspA) of Escherichia coli

Guest, John R.; Roberts, Ruth E.; Wilde, Robin J.

doi:10.1099/00221287-130-5-1271

Cited by 19 publications

(15 citation statements)

References 26 publications

(27 reference statements)

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“…The aspA gene encoding aspartase has been cloned and sequenced from several different bacterial sources (Guest et al, 1984;Takagi and Kisumi, 1985;Takagi et al, 1986a;Sun and Setlow, 1991). The aspA gene in E. coli encodes a 478 amino acid protein with a subunit molecular weight of 52 kDa , and the catalytically active enzyme is a tetramer composed of identical subunits (Williams and Lartigue, 1967).…”

Section: E Sequence Homologymentioning

confidence: 99%

L ‐Aspartase: New Tricks from an Old Enzyme

Viola

2000

Advances in Enzymology - And Related Areas of Molecular Biology

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Section: E Sequence Homologymentioning

confidence: 99%

L ‐Aspartase: New Tricks from an Old Enzyme

Viola

2000

Advances in Enzymology - And Related Areas of Molecular Biology

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“…coli cannot ferment glycerol anaerobically and requires the presence of a suitable electron acceptor such as fumarate for growth on this substrate (18). Asparagine can be converted to aspartate by asparaginase (4) and thence to the alternative electron acceptor fumarate by aspartase (14). Fumarate could be replaced by either of these amino acids for the anaerobic growth of wild-type E. coli on glycerol (Table 5).…”

Section: Methodsmentioning

confidence: 99%

Anaerobically induced genes of Escherichia coli

Winkelman¹,

Clark²

1986

J Bacteriol

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A collection of anaerobically induced gene fusions.were isolated, and representative isolates were characterized with respect to their regulatory properties, phenotypes, and approximate map locations. Four fusion strains that had defects in the anaerobic metabolism of asparagine or aspartate were found. These fusions were all repressed by alternate electron acceptors, ammonia, and glucose but were induced by other sugars. Several other fusion strains which demonstrated no observable phenotype showed diverse regulatory responses. The anaerobically induced fusions were scattered around the Escherichia coli chromosome more or less at random, suggesting that aUl the isolates examined were in separate genes.The natural habitat ofEscherichia coli is the large intestine of humans and other animals, from which E. coli emerged to colonize the scientific laboratory about half a century ago. Although the exact nature of the nutrients used by E. coli in the Wild remains obscure (20), it is clear that growth normally occurs in the absence of oxygen and that energy must be supplied either by fermentation or by the anaerobic respiration of alternative electron acceptors such as nitrate (15), fumarate (13, 17), trimethylamine oxide (TMAO) (23,32), or dimethyl sulfoxide (DMSO) (2). Work on E. coli and Salmonella typhimurium has established a large group of genes which are.involved in anaerobic respiration (13,15,31). These genes are repressed by oxygen (26, 31) and require the presence of the appropriate electron acceptor as an inducer (30). In addition, the product of thefnr gene (oxrA in S. typhimurium) appears to be an activator protein, necessary for transcription of many anaerobically regulated genes, including those involved in anaerobic respiration (7,27,28) and several others such as pepT of S. typhimurium (16,31 We previously demonstrated by using gene fusions that E. coli has approximately 50 anaerobically regulated genes, mnost of which are unmapped and biochemically uncharacterized (10). Our first collection of anaerobic gene fusions was made with the original Mu dl phage of Casadaban (3) and proved to be too unstable for convenient further characterization. We therefore made a second collection of anaerobically induced gene fusions by using the modified phage, Mu

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“…Of those with a known function, yfiA (translational stimulator ; Bylund et al, 1997), tufA\tufB (EF-Tu ; reviewed by Weijland et al, 1992) and yjbC (putative pseudouridylate synthase, shows similarity to rsuA ; Wrzesinski et al, 1995) encode proteins involved in translation ; this adaptation may comprise a general response to stress or may merely be a function of lower growth rates in the presence of a toxic agent. In addition, tnaA (tryptophanase ; Deeley & Yanofsky, 1981) and aspA (aspartase ; Guest et al, 1984) are reduced, suggesting the cell is less catabolic in nature.…”

Section: Transcriptional Analysis Of Adapted Strainsmentioning

confidence: 99%

Metal-ion tolerance in Escherichia coli: analysis of transcriptional profiles by gene-array technology

Brocklehurst

Morby

2000

Microbiology

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Escherichia coli was adapted to grow in medium containing substantially elevated concentrations of either Zn(II), Cd(II), Co(II) or Ni(II). Whole-genome transcriptional profiles were generated from adapted strains and analysed for significant alteration in transcript abundance with reference to a wild-type strain. Similar alterations in specific message levels were observed for strains adapted to the four metal ions. One unexpected trend was the increase in transcript level of genes involved in transposition of IS elements, particularly insA. Subsequent expression of insA-7 from a heterologous promoter in E. coli conferred tolerance to Zn(II).

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Cloning of the Aspartase Gene (aspA) of Escherichia coli

Cited by 19 publications

References 26 publications

L ‐Aspartase: New Tricks from an Old Enzyme

L ‐Aspartase: New Tricks from an Old Enzyme

Anaerobically induced genes of Escherichia coli

Metal-ion tolerance in Escherichia coli: analysis of transcriptional profiles by gene-array technology

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