A molecular analysis of the 53.3 minute region of the Escherichia coli linkage map

Andrews, Simon C.; Harrison, Pauline M.; Guest, John R.

doi:10.1099/00221287-137-2-361

Cited by 29 publications

(22 citation statements)

References 27 publications

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“…A previous sequence analysis of the 55.8 min region (formerly 53-3 min) of the E. coli genome revealed two ORFs (designated orf3 and orf4) that appeared to be the proximal cistrons of an unidentified operon (Andrews et al, 1991). The predicted orf3 product (ORF3) resembled the 16Fe ferredoxin subunit (DmsB) of the anaerobic dimethylsulphoxide reductase of E. coli, whereas the 34 codon partial sequence of orf4 indicated that it encodes a hydrophobic polypeptide.…”

Section: Resultsmentioning

confidence: 99%

“…Plasmid pLC25-14 was from the Clarke-Carbon ColEl-based library of E . coli chromosomal DNA (Clarke & Carbon, 1976;Andrews et al, 1991). The M13mp18 derivative, GS265, was produced by cloning the 4.3 kb BamHI fragment of pLC25-14 into the corresponding site of M13mp18 (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…In a previous report, two putative 07'-dependent promoters and potential FNR, CRP and Fur sites were detected upstream of the hyfcoding regions (Andrews et al, 1991). Further inspection of this region revealed a potential a5*-dependent promoter, ATGGCAT-5-ATGCA (1210-1226 bp, conserved residues in large caps; Thony & Hennecke, 1989) GTCGA ; TTTCGT/,C (underscored residues not conserved in the hyfsequence) ; and TGTC-GACA (the two half-sites are present in the opposite order in the hyf sequence) (Schlensog et al, 1994 …”

Section: Tabre 3 Predicted Membrane-spanning A-helicesmentioning

confidence: 99%

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A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system

et al. 1997

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The nucleotide sequence has been determined for a twelve-gene operon of Escherichia coli designated the hyf operon (hyfASCD€FGH/R-focB). The hyf operon is located a t 5508-56.0 min and encodes a putative nine-subunit hydrogenase complex (hydrogenase four or Hyf), a potential formate-and 6%-dependent transcriptional activator, HyfR (related to FhIA), and a possible formate transporter, FocB (related to FocA). Five of the nine Hyf-complex subunits are related to subunits of both the E. coli hydrogenase-3 complex (Hyc) and the proton-translocating NADH : quinone oxidoreductases (complex I and Nuo), whereas two Hyf subunits are related solely to NADH : quinone oxidoreductase subunits. The Hyf components include a predicted 523 residue [Ni-Fe] hydrogenase (large subunit) with an N-terminus (residues homologous to the 30 kDa or NuoC subunit of complex 1. It is proposed that Hyf, in conjunction with formate dehydrogenase H (Fdh-H), forms a hitherto unrecognized respiration-linked proton-translocating formate hydrogenlyase (FHL-2). It is likely that HyfR acts as a formate-dependent regulator of the hyf operon and that FocB provides the Hyf complex with external formate as substrate.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Tabre 3 Predicted Membrane-spanning A-helicesmentioning

confidence: 99%

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A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system

et al. 1997

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“…Genetic organization of the dapE-dapA region of the E. coli chromosome. The sequencing data reported in this paper and others (1,3,28,33) have been correlated (thick bars) with the updated physical map of this region (17). Only the restriction sites present in the sequenced regions are shown.…”

Section: Resultsmentioning

confidence: 99%

“…The carboxy terminus of its putative product is highly similar to the carboxy terminus of the E. coli envD gene product (13), with 24 identical and 6 similar residues out of 35 (data not shown). These sequencing data have been combined with results obtained for the neighboring dapA region (1,3,28,33) and correlated with the physical map of the E. coli chromosome (17) (Fig. 3).…”

Section: Resultsmentioning

confidence: 99%

Cloning, characterization, and expression of the dapE gene of Escherichia coli

et al. 1992

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The dapE gene of Escherichia coli encodes N-succinyl-L-diaminopimelic acid desuccinylase, an enzyme that catalyzes the synthesis of LL-diaminopimelic acid, one of the last steps in the diaminopimelic acid-lysine pathway. The dapE gene region was previously purified from a lambda bacteriophage transducing the neighboring purC gene (J. Parker, J. Bacteriol. 157:712-717, 1984). Various subcloning steps led to the identification of a 2.3-kb fragment that complemented several dapE mutants and allowed more than 400-fold overexpression of N-succinyl-L-diaminopimelic acid desuccinylase. Sequencing of this fragment revealed the presence of two closely linked open reading frames. The second one encodes a 375-residue, 41,129-M(r) polypeptide that was identified as N-succinyl-L-diaminopimelic acid desuccinylase. The first one encodes a 118-residue polypeptide that is not required for diaminopimelic acid biosynthesis, as judged by the wild-type phenotype of a strain in which this gene was disrupted. Expression of the dapE gene was studied by monitoring amylomaltase activity in strains in which the malPQ operon was under the control of various fragments located upstream of the dapE gene. The major promoter governing dapE transcription was found to be located in the adjacent orf118 gene, while a minor promoter allowed the transcription of both orf118 and dapE. Neither of these two promoters is regulated by the lysine concentration in the growth medium.

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Physiological Roles of a Periodontopathic Bacterial Membrane-Bound Quinol Peroxidase

Kawai

2013

Studies on Periodontal Disease

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A molecular analysis of the 53.3 minute region of the Escherichia coli linkage map

Cited by 29 publications

References 27 publications

A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system

A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system

Cloning, characterization, and expression of the dapE gene of Escherichia coli

Physiological Roles of a Periodontopathic Bacterial Membrane-Bound Quinol Peroxidase

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