scholarly journals Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli

1984 ◽  
Vol 222 (2) ◽  
pp. 519-534 ◽  
Author(s):  
D Wood ◽  
M G Darlison ◽  
R J Wilde ◽  
J R Guest
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Succinate Dehydrogenase ◽  
Citrate Synthase ◽  
Attachment Site ◽  
Fumarate Reductase ◽  
Receptor Protein ◽  
Base Pairs ◽  
Gene Encoding ◽  
Active Site Cysteine

The nucleotide sequence of a 3614 base-pair segment of DNA containing the sdhA gene, encoding the flavoprotein subunit of succinate dehydrogenase of Escherichia coli, and two genes sdhC and sdhD, encoding small hydrophobic subunits, has been determined. Together with the iron-sulphur protein gene (sdhB) these genes form an operon (sdhCDAB) situated between the citrate synthase gene (gltA) and the 2-oxoglutarate dehydrogenase complex genes (sucAB): gltA-sdhCDAB-sucAB. Transcription of the gltA and sdhCDAB gene appears to diverge from a single intergenic region that contains two pairs of potential promoter sequences and two putative CRP (cyclic AMP receptor protein)-binding sites. The sdhA structural gene comprises 1761 base-pairs (587 codons, excluding the initiation codon, AUG) and it encodes a polypeptide of Mr 64268 that is strikingly homologous with the flavoprotein subunit of fumarate reductase (frdA gene product). The FAD-binding region, including the histidine residue at the FAD-attachment site, has been identified by its homology with other flavoproteins and with the flavopeptide of the bovine heart mitochondrial succinate dehydrogenase. Potential active-site cysteine and histidine residues have also been indicated by the comparisons. The sdhC (384 base-pairs) and sdhD (342 base-pairs) structural genes encode two strongly hydrophobic proteins of Mr 14167 and 12792 respectively. These proteins resemble in size and composition, but not sequence, the membrane anchor proteins of fumarate reductase (the frdC and frdD gene products).

scholarly journals Nucleotide sequence for the hemD gene of Escherichia coli encoding uroporphyrinogen III synthase and initial evidence for a hem operon

1988 ◽  
Vol 249 (2) ◽  
pp. 613-616 ◽  
Author(s):  
P M Jordan ◽  
B I A Mgbeje ◽  
S D Thomas ◽  
A F Alwan
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Close Agreement ◽  
Chromosome 2 ◽  
Base Pairs ◽  
Gene Encoding ◽  
E Coli ◽  
Entire Nucleotide Sequence

1. The hemD gene, encoding uroporphyrinogen III synthase, has been located adjacent to the hemC gene at 85 min on the Escherichia coli chromosome. 2. The entire nucleotide sequence (741 base pairs) of the hemD gene is reported. 3. E. coli strains harbouring plasmics containing the hemD gene produce greatly elevated levels of uroporphyrinogen III synthase. 4. Purified uroporphyrinogen III synthase, isolated from the hemD-containing strain ST1046, has an Mr of 29,000, in close agreement with that predicted from the nucleotide sequence. 5. The existence of a hem operon is suggested.

Nucleotide sequence of the murE gene of Escherichia coli

1989 ◽  
Vol 35 (11) ◽  
pp. 1051-1054 ◽  
Author(s):  
Jing-Song Tao ◽  
Edward E. Ishiguro
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Diaminopimelic Acid ◽  
Amino Acid Residues ◽  
Penicillin Binding Protein ◽  
Coding Region ◽  
Base Pairs ◽  
Gene Encoding ◽  
Peptidoglycan Synthesis

The nucleotide sequence of the murE gene encoding the diaminopimelic acid adding enzyme of Escherichia coli is reported. The coding region consisted of 1413 base pairs and was separated from the ftsI (penicillin-binding protein 3) gene by 61 base pairs. The deduced primary structure of MurE comprised 471 amino acid residues with a molecular mass of 50.6 kilodaltons.Key words: Escherichia coli, murE, peptidoglycan synthesis, diaminopimelic acid adding enzyme.

scholarly journals Nucleotide sequence of the promoter region of the citrate synthase gene (gltA) of Escherichia coli

FEBS Letters ◽  
1983 ◽  
Vol 156 (2) ◽  
pp. 366-370 ◽  
Author(s):  
Elizabeth P. Hull ◽  
Margaret E. Spencer ◽  
David Wood ◽  
John R. Guest
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Promoter Region ◽  
Citrate Synthase

Nucleotide sequence of the cybB gene encoding cytochrome b 561 in Escherichia coli K12

1988 ◽  
Vol 212 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Hiro Nakamura ◽  
Hiroshi Murakami ◽  
Ichiro Yamato ◽  
Yasuhiro Anraku
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Cytochrome B ◽  
Gene Encoding ◽  
Escherichia Coli K12 ◽  
Cybb Gene

scholarly journals GadY, a Small-RNA Regulator of Acid Response Genes in Escherichia coli

2004 ◽  
Vol 186 (20) ◽  
pp. 6698-6705 ◽  
Author(s):  
Jason A. Opdyke ◽  
Ju-Gyeong Kang ◽  
Gisela Storz
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Small Rna ◽  
Acid Resistance ◽  
Base Pairs ◽  
Gene Encoding ◽  
Mrna Accumulation ◽  
Long Form ◽  
Genes Encoding ◽  
Opposite Strand

ABSTRACT A previous bioinformatics-based search for small RNAs in Escherichia coli identified a novel RNA named IS183. The gene encoding this small RNA is located between and on the opposite strand of genes encoding two transcriptional regulators of the acid response, gadX (yhiX) and gadW (yhiW). Given that IS183 is encoded in the gad gene cluster and because of its role in regulating acid response genes reported here, this RNA has been renamed GadY. We show that GadY exists in three forms, a long form consisting of 105 nucleotides and two processed forms, consisting of 90 and 59 nucleotides. The expression of this small RNA is highly induced during stationary phase in a manner that is dependent on the alternative sigma factor σS. Overexpression of the three GadY RNA forms resulted in increased levels of the mRNA encoding the GadX transcriptional activator, which in turn caused increased levels of the GadA and GadB glutamate decarboxylases. A promoter mutation which abolished gadY expression resulted in a reduction in the amount of gadX mRNA during stationary phase. The gadY gene was shown to overlap the 3′ end of the gadX gene, and this overlap region was found to be necessary for the GadY-dependent accumulation of gadX mRNA. We suggest that during stationary phase, GadY forms base pairs with the 3′-untranslated region of the gadX mRNA and confers increased stability, allowing for gadX mRNA accumulation and the increased expression of downstream acid resistance genes.

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