The organization and nucleotide sequence of the Bacillus subtilis hisH, tyrA and aroE genes

Henner, Dennis J.; Band, Louise; Flaggs, G.; Chen, Ellson

doi:10.1016/0378-1119(86)90394-x

Cited by 46 publications

(33 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ORF was terminated at the codon TAA. A search of GenBank revealed a 35% identity of this deduced peptide with the product of the Bacillus subtilis hisH gene [31]. This alignment is shown in Fig.…”

Section: Identity Of An Incomplete O W Upstream Of Tyrcmentioning

confidence: 81%

“…5. This gene arrangement could suggest the existence of a counterpart to the trpA-hisH-tyrA-aroE gene organization present in B. subtilis [31]. Alternatively, the aminotransferase may function in vivo as an aromatic aminotransferase, and it may be coincidental that the deduced amino-acid sequence shows greater identity to HisH than to AroB.…”

Section: Identity Of An Incomplete O W Upstream Of Tyrcmentioning

confidence: 99%

“…The pairwise alignment of the cyclohexadienyl-dehydrogenase sequence with the C-terminal portion of the T-proteins of E. coli [29] and E. herbicola [33], and prephenate dehydrogenases of B. subtilis [31] and S. cerevisiae [321 was performed using the GAP program (GCG). The cyclohexadienyl dehydrogenase showed only 21 % identity with the Tprotein of E. coli, 23% identity with the T-protein of E. herbicola, 19% identity with the prephenate dehydrogenase of S. cerevisiue, but 32% identity with the prephenate dehydrogenase of B. subtilis.…”

mentioning

confidence: 99%

See 2 more Smart Citations

An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis

Zhao

Xia

Ingram

et al. 1993

European Journal of Biochemistry

View full text Add to dashboard Cite

The key enzyme of tyrosine biosynthesis in many Gram-negative prokaryotes is cyclohexadienyl dehydrogenase. The Zymomonas mobilis gene ( t y r o coding for this enzyme was cloned in Escherichia coli by camplementation of a tyrosine auxotroph. The tyrC gene was 882 bp long, encoding a protein with a calculated molecular mass of 32086 Da. The Z. mobilis cyclohexadienyl dehydrogenase expressed in E. coli was purified to electrophoretic homogeneity. The subunit molecular mass of the purified enzyme was 32kDa as determined by SDSPAGE. The ratio of the activity of arogenate dehydrogenase to that of prephenate dehydrogenase (approximately 3 : 1) remained constant throughout purification, and the two activities were therefore inseparable. The genetic and biochemical data obtained demonstrated a single enzyme protein capable of catalyzing either of two reactions. K, values of 0.25 mM and 0.18 mM were obtained for prephenate and L-arogenate, respectively. The K, value obtained for NAD+ (0.09 mM) was the same regardless of whether the enzyme was assayed as arogenate dehydrogenase or as prephenate dehydrogenase. Unlike the corresponding enzyme of Pseudomonas aemginosa or E. coli, the cyclohexadienyl dehydrogenase of Z. mobilis lacks sensitivity to feedback inhibition by L-tyrosine. A typical NAD+-binding domain was found to be located at the N-terminus of the protein.Although the deduced amino-acid sequence of the Z. mobilis cyclohexadienyl dehydrogenase showed relatively low identity (19-32 %) with the prephenate dehydrogenases of Bacillus subtilis and Saccharomyces cerevisiae, as well as with the cyclohexadienyl dehydrogenase components of the bifunctional T-proteins of E. coli and Erwinia herbicola, a presumptive motif was identified which may correspond to critical residues of the binding site for cyclohexadienyl substrate molecules.Immediately upstream of tyrC a portion of a gene was sequenced and found to exhibit clearcut homology of the deduced amino-acid sequence with the B. subtilis hzsH gene product. Thus, the Zymomonas gene organization is reminiscent of the linkage of genes encoding a tyrosine-pathway dehydrogenase and a histidine-pathway aminotransferase in B. subtilis.

show abstract

Section: Identity Of An Incomplete O W Upstream Of Tyrcmentioning

confidence: 81%

Section: Identity Of An Incomplete O W Upstream Of Tyrcmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis

Zhao

Xia

Ingram

et al. 1993

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…There are several possible reasons for this. For instance, the groupings depicted may simply reflect the fact that in fungi, the EPSP synthase is part of a pentafunctional enzyme, AROM, expressed as a polyprotein encoded by the AROl gene (Charles et al, 1986;Duncan et al, 1987), while in bacteria and plants the EPSP synthase enzyme is encoded by an individual aroA structural gene (Klee et al, 1987;Gasser et al, 1988;Henner et al, 1986;Maskell et al, 1988;O'Gaora et al, 1989;Duncan et al, 1984;Stalker et al, 1985). Our findings also support the hypothesis that plastids in plants are descendants of endosymbiotic prokaryotes that invaded ancestral plant cells (Margulis, 1970).…”

Section: Dna Sequence Analysismentioning

confidence: 99%

Cloning and DNA sequence analysis of the serC-aroA operon from Salmonella gallinarum; evolutionary relationships between the prokaryotic and eukaryotic aro A-encoded enzymes

Griffin¹,

Griffin²

1991

Microbiology

View full text Add to dashboard Cite

The serC-aroA operon of Salmonella galfinarum was isolated from a gene library using a labelled oligonucleotide probe and by complementation of an aroA Escherichia cofi strain. The nucleotide sequence of a 2.6 kbp fragment was determined. The predicted amino acid sequence of the aroA gene product was compared to the equivalent sequence from ten other organisms. Computer-generated evolutionary trees clearly divide the eleven sequences into four different groups: Gram-negative bacteria, Gram-positive bacteria, fungi and plants. These trees depict a close evolutionary relationship between the sequences from Gram-negative bacteria and higher plants.

show abstract

“…In Staphylococcus aureus, six of the genes (hisE, -A, -B, -C, -D, and -G) are clustered, whereas in Streptomyces coelicolor, five (and possibly six) genes (hisD, -C, -B, -H, -A, and possibly -F) form an operon and two (hisIE and hisB) are independent (30,36). In Bacillus subtilis, the genes map in two locations, one grouping seven genes (hisA, -B, -D, -F, -G, -C, and -IE) and the other containing a single gene (hisH, corresponding to hisC in E. coli) (11,18,25,37). The hisI gene from a methanogenic archaebacterium is separated from the other his genes (6).…”

mentioning

confidence: 99%

Histidine biosynthesis genes in Lactococcus lactis subsp. lactis

1992

View full text Add to dashboard Cite

The genes of Lactococcus lactis subsp. lactis involved in histidine biosynthesis were cloned and characterized by complementation of Escherichia coli and Bacilus subtUlis mutants and DNA sequencing. Complementation of E. coli hisA, hisB, hisC, hisD, hisF, hisG, and hisIE genes and the B. subtilis hisH gene (the E. coli hisC equivalent) allowed localization of the corresponding lactococcal genes. Nucleotide sequence analysis of the 11.5-kb lactococcal region revealed 14 open reading frames (ORFs), 12 of which might form an operon. The putative operon includes eight ORFs which encode proteins homologous to enzymes involved in histidine biosynthesis. The operon also contains (i) an ORF encoding a protein homologous to the histidyl-tRNA synthetases but lacking a motif implicated in synthetase activity, which suggests that it has a role different from tRNA aminoacylation, and (ii) an ORF encoding a protein that is homologous to the 3'-aminoglycoside phosphotransferases but does not confer antibiotic resistance. The remaining ORFs specify products which have no homology with proteins in the EMBL and GenBank data bases.

show abstract

The organization and nucleotide sequence of the Bacillus subtilis hisH, tyrA and aroE genes

Cited by 46 publications

References 13 publications

An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis

An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis

Cloning and DNA sequence analysis of the serC-aroA operon from Salmonella gallinarum; evolutionary relationships between the prokaryotic and eukaryotic aro A-encoded enzymes

Histidine biosynthesis genes in Lactococcus lactis subsp. lactis

Contact Info

Product

Resources

About