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.

scholarly journals Characterization and Complete Genome Analysis of a Novel Escherichia Phage, vB_EcoM-RPN242

2022 ◽  
Author(s):  
Napakhwan Imklin ◽  
Pattaraporn Sripras ◽  
Narut Thanantong ◽  
Porntippa Lekcharoensuk ◽  
Rujikan Nasanit
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Sequence Comparison ◽  
The Novel ◽  
Base Pairs ◽  
E Coli ◽  
Double Stranded Dna ◽  
Protein Encoding ◽  
Encoding Genes ◽  
Complete Genome Analysis

Abstract The novel Escherichia phage vB_EcoM-RPN242 was isolated using a strain of Escherichia coli host originated from a diarrheal piglet. The phage was able to form plaques on the E. coli lawn at 15−45ºC. Moreover, it was stable over a wide pH (4−10) and temperature (4−70ºC) range. The vB_EcoM-RPN242 genome was found to be a linear, double-stranded DNA consisting of 154,840 base pairs. There were 195 protein-encoding genes and 2 tRNAs detected in the genome, however no unfavorable gene was found. According to the overall nucleotide sequence comparison, the vB_EcoM-RPN242 possibly represents a new phage species in the genus Agtrevirus.

Plasmid-directed synthesis of genuine adenovirus 2 early-region 1A and 1B proteins in Escherichia coli

1984 ◽  
Vol 4 (8) ◽  
pp. 1427-1439
Author(s):  
J L Ko ◽  
M L Harter
Keyword(s):  
Escherichia Coli ◽  
Tumor Antigens ◽  
Human Adenovirus ◽  
Cellular Protein ◽  
T Antigen ◽  
Sequencing Analysis ◽  
Gene Encoding ◽  
E Coli ◽  
Dna Sequencing Analysis ◽  
Entire Nucleotide Sequence

The transforming region of human adenovirus 2 is located in the left 11.2% of the viral genome and is comprised of two distinct genetic units termed E1A and E1B. cDNAs containing the entire nucleotide sequence of the mature E1A 13S and E1B 22S mRNAs that are complementary to these genetic units have been introduced into bacterial plasmids a short distance downstream from the Escherichia coli lac promoter. Upon transformation into appropriate E. coli hosts, one of these plasmids, pKHAO, directed the synthesis of a 45-kilodalton (kd) protein, and the other, pKHBO, synthesized a protein of 54.9 kd. Both of these plasmid-encoded proteins constituted 0.1 to 0.3% of the total cellular protein and were virtually identical to the authentic adenovirus 2 E1A 42- to 50-kd and E1B 53- to 58-kd tumor antigens (T antigen) as determined by gel electrophoresis, immunoprecipitation, and tryptic fingerprint analysis. With the use of our pKHBO expression plasmid we were also able to demonstrate that the second AUG sequence appearing in the E1B 22S mRNA corresponded to the start of the gene encoding the large adenovirus 2 T antigen. This confirms theoretical deductions based on DNA sequencing analysis that translation of the large T antigen initiates translation at an internal ATG rather than at the 5'-proximal AUG.

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 Plasmid-directed synthesis of genuine adenovirus 2 early-region 1A and 1B proteins in Escherichia coli.

1984 ◽  
Vol 4 (8) ◽  
pp. 1427-1439 ◽  
Author(s):  
J L Ko ◽  
M L Harter
Keyword(s):  
Escherichia Coli ◽  
Tumor Antigens ◽  
Human Adenovirus ◽  
Cellular Protein ◽  
T Antigen ◽  
Sequencing Analysis ◽  
Gene Encoding ◽  
E Coli ◽  
Dna Sequencing Analysis ◽  
Entire Nucleotide Sequence

The transforming region of human adenovirus 2 is located in the left 11.2% of the viral genome and is comprised of two distinct genetic units termed E1A and E1B. cDNAs containing the entire nucleotide sequence of the mature E1A 13S and E1B 22S mRNAs that are complementary to these genetic units have been introduced into bacterial plasmids a short distance downstream from the Escherichia coli lac promoter. Upon transformation into appropriate E. coli hosts, one of these plasmids, pKHAO, directed the synthesis of a 45-kilodalton (kd) protein, and the other, pKHBO, synthesized a protein of 54.9 kd. Both of these plasmid-encoded proteins constituted 0.1 to 0.3% of the total cellular protein and were virtually identical to the authentic adenovirus 2 E1A 42- to 50-kd and E1B 53- to 58-kd tumor antigens (T antigen) as determined by gel electrophoresis, immunoprecipitation, and tryptic fingerprint analysis. With the use of our pKHBO expression plasmid we were also able to demonstrate that the second AUG sequence appearing in the E1B 22S mRNA corresponded to the start of the gene encoding the large adenovirus 2 T antigen. This confirms theoretical deductions based on DNA sequencing analysis that translation of the large T antigen initiates translation at an internal ATG rather than at the 5'-proximal AUG.

scholarly journals Pea chloroplast DNA encodes homologues of Escherichia coli ribosomal subunit S2 and the β'-subunit of RNA polymerase

1986 ◽  
Vol 236 (2) ◽  
pp. 453-460 ◽  
Author(s):  
A L Cozens ◽  
J E Walker
Keyword(s):  
Escherichia Coli ◽  
Nucleotide Sequence ◽  
Rna Polymerase ◽  
Atp Synthase ◽  
Ribosomal Subunit ◽  
Beta Subunit ◽  
Β Subunit ◽  
Membrane Domain ◽  
Gene Encoding ◽  
E Coli

The nucleotide sequence has been determined of a segment of 4680 bases of the pea chloroplast genome. It adjoins a sequence described elsewhere that encodes subunits of the F0 membrane domain of the ATP-synthase complex. The sequence contains a potential gene encoding a protein which is strongly related to the S2 polypeptide of Escherichia coli ribosomes. It also encodes an incomplete protein which contains segments that are homologous to the beta'-subunit of E. coli RNA polymerase and to yeast RNA polymerases II and III.

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.

The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms

Microbiology ◽  
2005 ◽  
Vol 151 (5) ◽  
pp. 1421-1431 ◽  
Author(s):  
Patrice Bruscella ◽  
Laure Cassagnaud ◽  
Jeanine Ratouchniak ◽  
Gaël Brasseur ◽  
Elisabeth Lojou ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acidithiobacillus Ferrooxidans ◽  
Biochemical Properties ◽  
Gene Encoding ◽  
Iron Sulfur Cluster ◽  
E Coli ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Tat System ◽  
Micro Organisms

The gene encoding a putative high-potential iron–sulfur protein (HiPIP) from the strictly acidophilic and chemolithoautotrophic Acidithiobacillus ferrooxidans ATCC 33020 has been cloned and sequenced. This potential HiPIP was overproduced in the periplasm of the neutrophile and heterotroph Escherichia coli. As shown by optical and EPR spectra and by electrochemical studies, the recombinant protein has all the biochemical properties of a HiPIP, indicating that the iron–sulfur cluster was correctly inserted. Translocation of this protein in the periplasm of E. coli was not detected in a ΔtatC mutant, indicating that it is dependent on the Tat system. The genetic organization of the iro locus in strains ATCC 23270 and ATCC 33020 is different from that found in strains Fe-1 and BRGM. Indeed, in A. ferrooxidans ATCC 33020 and ATCC 23270 (the type strain), iro was not located downstream from purA but was instead downstream from petC2, encoding cytochrome c 1 from the second A. ferrooxidans cytochrome bc 1 complex. These findings underline the genotypic heterogeneity within the A. ferrooxidans species. The results suggest that Iro transfers electrons from a cytochrome bc 1 complex to a terminal oxidase, as proposed for the HiPIP in photosynthetic bacteria.

scholarly journals Alleviation of C⋅C Mismatches in DNA by the Escherichia coli Fpg Protein

2021 ◽  
Vol 12 ◽  
Author(s):  
Almaz Nigatu Tesfahun ◽  
Marina Alexeeva ◽  
Miglė Tomkuvienė ◽  
Aysha Arshad ◽  
Prashanna Guragain ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Excision Repair ◽  
Dna Lesions ◽  
Base Pairs ◽  
E Coli ◽  
Thymine Glycol ◽  
Base Excision ◽  
The Cost ◽  
Primary Substrate

DNA polymerase III mis-insertion may, where not corrected by its 3′→ 5′ exonuclease or the mismatch repair (MMR) function, result in all possible non-cognate base pairs in DNA generating base substitutions. The most thermodynamically unstable base pair, the cytosine (C)⋅C mismatch, destabilizes adjacent base pairs, is resistant to correction by MMR in Escherichia coli, and its repair mechanism remains elusive. We present here in vitro evidence that C⋅C mismatch can be processed by base excision repair initiated by the E. coli formamidopyrimidine-DNA glycosylase (Fpg) protein. The kcat for C⋅C is, however, 2.5 to 10 times lower than for its primary substrate 8-oxoguanine (oxo8G)⋅C, but approaches those for 5,6-dihydrothymine (dHT)⋅C and thymine glycol (Tg)⋅C. The KM values are all in the same range, which indicates efficient recognition of C⋅C mismatches in DNA. Fpg activity was also exhibited for the thymine (T)⋅T mismatch and for N4- and/or 5-methylated C opposite C or T, Fpg activity being enabled on a broad spectrum of DNA lesions and mismatches by the flexibility of the active site loop. We hypothesize that Fpg plays a role in resolving C⋅C in particular, but also other pyrimidine⋅pyrimidine mismatches, which increases survival at the cost of some mutagenesis.

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