scholarly journals Cloning and nucleotide sequence of the gyrA gene from Campylobacter fetus subsp. fetus ATCC 27374 and characterization of ciprofloxacin-resistant laboratory and clinical isolates.

1997 ◽  
Vol 41 (3) ◽  
pp. 665-671 ◽  
Author(s):  
D E Taylor ◽  
A S Chau
Keyword(s):  
Nucleotide Sequence ◽  
Dna Gyrase ◽  
Amino Acid Identity ◽  
Gyra Gene ◽  
Reading Frame ◽  
B Subunit ◽  
Campylobacter Fetus ◽  
A Subunit ◽  
Fetus Subsp ◽  
Genomic Map

The gyrA gene of Campylobacter fetus subsp. fetus, which encodes the A subunit of DNA gyrase, was cloned, and its nucleotide sequence was determined. An open reading frame of 2,586 nucleotides which encodes a polypeptide of 862 amino acids with an Mr of 96,782 was identified. C. fetus subsp. fetus GyrA is most closely related to Campylobacter jejuni GyrA, with 73% homology at the nucleotide level and 78% identity between polypeptides. The next most closely related GyrA was that from Helicobacter pylori, with both DNA homology and amino acid identity of 63%. The gyrA and gyrB (DNA gyrase B subunit) genes were located on the genomic map of C. fetus subsp. fetus ATCC 27374 and shown to be separate. A clinical isolate of C. fetus subsp. fetus and a laboratory-derived mutant of ATCC 27374, both resistant to ciprofloxacin, had identical mutations within the quinolone resistance determining region. In both mutants a G-->T transversion, corresponding to a substitution of Asp-91 to Tyr in GyrA, was linked to ciprofloxacin resistance, giving MICs of 8 to 16 micrograms/ml.

Changed properties of the A subunit in DNA gyrase with a B subunit mutation

1982 ◽  
Vol 186 (4) ◽  
pp. 572-574 ◽  
Author(s):  
E. S. Bogdanova ◽  
S. M. Mirkin ◽  
Zh. G. Shmerling
Keyword(s):  
Dna Gyrase ◽  
B Subunit ◽  
A Subunit

4-(tert-butyl)-N,N-diethylbenzenesulfonamide: Structural, absorption distribution metabolism excretion toxicity (ADMET) and molecular docking studies

2021 ◽  
pp. 329-336 ◽  
Author(s):  
Gurumallappa Gurumallappa ◽  
Jayashankar Jayaprakash ◽  
Ananda A. Puttaswamy ◽  
Jayanth H. Sunderraj ◽  
Puttaswamappa Mallu ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Title Compound ◽  
Living Organism ◽  
Dna Gyrase ◽  
Docking Studies ◽  
Monoclinic Crystal ◽  
Tert Butyl ◽  
B Subunit ◽  
A Subunit ◽  
Physical And Chemical

Sulfonamides are a very good antibacterial agent that targets essential bacterial enzymes specifically DNA gyrase. The objective of the present work was to investigate the molecular docking of the (4-(tert-butyl)-N,N-diethylbenzenesulfonamide) with the DNA gyrase of S. aureus. The energy-free topoisomerase activity of the A subunit, which breaks the DNA, is inhibited by 4-quilones such as nalidixic acid and ciprofloxacin. The energy transducing activity of the B subunit is inhibited by novobiocin and other coumarin antibiotics. Single crystal X-ray diffractometer study was carried out to understand the structure, physical and chemical reactive parameters, the title compound is crystallized under monoclinic crystal system with the space group of P21/C. To understand the behaviour of the title compound in living organism, Absorption, Distribution, Metabolism, Excretion analysis was done using Swiss ADME and Osiris data warrior tool. Further, Toxicity of the title compound was predicted by using PKCSM online software.

scholarly journals Mapping Simocyclinone D8 Interaction with DNA Gyrase: Evidence for a New Binding Site on GyrB

2009 ◽  
Vol 54 (1) ◽  
pp. 213-220 ◽  
Author(s):  
C. Sissi ◽  
E. Vazquez ◽  
A. Chemello ◽  
L. A. Mitchenall ◽  
A. Maxwell ◽  
...  
Keyword(s):  
Dna Gyrase ◽  
Coumarin Derivative ◽  
Streptomyces Antibioticus ◽  
B Subunit ◽  
Terminal Domain ◽  
Antiproliferative Agent ◽  
Gyrase A ◽  
A Subunit ◽  
The Individual ◽  
Simocyclinone D8

ABSTRACT Simocyclinone D8, a coumarin derivative isolated from Streptomyces antibioticus Tü 6040, represents an interesting new antiproliferative agent. It was originally suggested that this drug recognizes the GyrA subunit and interferes with the gyrase catalytic cycle by preventing its binding to DNA. To further characterize the mode of action of this antibiotic, we investigated its binding to the reconstituted DNA gyrase (A2B2) as well as to its GyrA and GyrB subunits and the individual domains of these proteins, by performing protein melting and proteolytic digestion studies as well as inhibition assays. Two binding sites were identified, one (anticipated) in the N-terminal domain of GyrA (GyrA59) and the other (unexpected) at the C-terminal domain of GyrB (GyrB47). Stabilization of the A subunit appears to be considerably more effective than stabilization of the B subunit. Our data suggest that these two distinct sites could cooperate in the reconstituted enzyme.

Nucleotide sequences of the 2-oxoacid ferredoxin oxidoreductase and ferredoxin genes fromFrankiastrain EuIK1, a symbiont ofElaeagnus umbellataroot nodules

1999 ◽  
Vol 77 (9) ◽  
pp. 1279-1286
Author(s):  
Won Young Yoo ◽  
Si Bum Sung ◽  
Chung Sun An
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Genomic Library ◽  
Sequence Similarity ◽  
Root Nodules ◽  
Amino Acid Sequences ◽  
Elaeagnus Umbellata ◽  
Ferredoxin Oxidoreductase ◽  
B Subunit ◽  
A Subunit

A genomic clone, pEuNIFII, was isolated by screening a genomic library of Frankia strain EuIK1, a symbiont of Elaeagnus umbellata Thunb. root nodules. A 1.5-kb fragment of pEuNIF4.0, which contained ORF2 and N-terminal part of nifS, was used as a probe. A 7.2-kb BamHI fragment of pEuNIFII, which was proven to be adjacent to the probe, was subjected to sequence determination. The sequence analysis suggested one partial ORF followed by three open reading frames (ORFs). Two ORFs next to nifS encodes an a subunit (672 amino acids) and b subunit (347 amino acids) of a 2-oxoacid ferredoxin oxidoreducatase (OR), respectively. The third ORF encodes 114 amino acids of a 7Fe-type ferredoxin (Fdx). All ORFs are transcribed in the same direction as other nif genes. Alignment of the deduced amino acid sequences from frankiae OR revealed the motifs of gamma and alpha domains seen in other ORs in the a subunit, and the beta domain in the b subunit. Frankia or shows about 44% nucleotide sequence similarity with nifJ from Klebsiella pneumoniae, while frankiae fdx shows about 56% similarity with fdxI from Azotobacter vinelandii. These genes are reported for the first time in Frankia, and putative roles of their products in symbiosis is discussed in relation to nitrogen fixation and carbohydrate metabolism.Key words: 2-oxoacid ferredoxin oxidoreductase, ferredoxin, nucleotide sequence, Frankia EuIK1.

scholarly journals Complete nucleotide sequence of Kashmir bee virus and comparison with acute bee paralysis virus

2004 ◽  
Vol 85 (8) ◽  
pp. 2263-2270 ◽  
Author(s):  
J. R. de Miranda ◽  
M. Drebot ◽  
S. Tyler ◽  
M. Shen ◽  
C. E. Cameron ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Identity ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Acid Identity ◽  
Kashmir Bee Virus ◽  
Acute Bee Paralysis Virus ◽  
Bee Virus ◽  
Paralysis Virus

The complete nucleotide sequence of a novel virus is presented here together with serological evidence that it belongs to Kashmir bee virus (KBV). Analysis reveals that KBV is a cricket paralysis-like virus (family Dicistroviridae: genus Cripavirus), with a non-structural polyprotein open reading frame in the 5′ portion of the genome separated by an intergenic region from a structural polyprotein open reading frame in the 3′ part of the genome. The genome also has a polyadenylated tail at the 3′ terminus. KBV is one of several related viruses that also includes acute bee paralysis virus (ABPV). Although KBV and ABPV are about 70 % identical over the entire genome, there are considerable differences between them in significant areas of the genome, such as the 5′ non-translated region (42 % nucleotide identity), between the helicase and 3C-protease domains of the non-structural polyprotein (57 % amino acid identity) and in a 90 aa stretch of the structural polyprotein (33 % amino acid identity). Phylogenetic analyses show that KBV and ABPV isolates fall into clearly separated clades with moderate evolutionary distance between them. Whether these genomic and evolutionary differences are sufficient to classify KBV and ABPV as separate species remains to be determined.

scholarly journals Cloning and Nucleotide Sequence of the DNA Gyrase gyrA Gene from Serratia marcescens and Characterization of Mutations in gyrA of Quinolone-Resistant Clinical Isolates

1998 ◽  
Vol 42 (1) ◽  
pp. 190-193 ◽  
Author(s):  
Jeong Hoon Kim ◽  
Eun Hee Cho ◽  
Kwang Seo Kim ◽  
Hak Yeop Kim ◽  
Young Min Kim
Keyword(s):  
Serratia Marcescens ◽  
Dna Gyrase ◽  
Quinolone Resistance ◽  
Clinical Isolates ◽  
Single Amino Acid ◽  
Common Mechanism ◽  
Temperature Sensitive ◽  
Gyra Gene ◽  
Calculated Molecular Mass ◽  
Reading Frame

ABSTRACT The sequence of the DNA gyrase gyrA gene ofSerratia marcescens ATCC 14756 was determined. An open reading frame of 2,640 nucleotides coding for a polypeptide with a calculated molecular mass of 97,460 was found, and its sequence complemented the sequence of an Escherichia coli gyrAtemperature-sensitive mutation. Analysis of the PCR products of the quinolone resistance-determining regions of gyrA genes from six quinolone-resistant clinical isolates revealed a single amino acid substitution, Ser-83 to Arg or Asp-87 to Tyr, in all six mutants, suggesting that a mutational alteration in gyrA is a common mechanism of quinolone resistance in S. marcescens.

Cloning and nucleotide sequence of the DNA gyrase gyrA gene from the fish pathogen Aeromonas salmonicida.

1996 ◽  
Vol 40 (5) ◽  
pp. 1126-1133 ◽  
Author(s):  
H Oppegaard ◽  
H Sørum
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Dna Gyrase ◽  
Aeromonas Salmonicida ◽  
Fish Pathogen ◽  
Gyra Gene ◽  
Calculated Molecular Mass ◽  
Gyrase A

The DNA gyrase gyrA gene from the fish pathogen Aeromonas salmonicida 2148/89 was cloned, and the nucleotide sequence was determined. An open reading frame of 2,766 nucleotides was identified and was found to encode a protein of 922 amino acids with a calculated molecular mass of 101.1 kDa. The derived amino acid sequence shared a high degree of identity with other DNA gyrase A proteins, in particular, with other gram-negative GyrA sequences. When the amino acid sequence of A. salmonicida GyrA was compared with that of Escherichia coli GyrA, a number of conserved residues were present at identical coordinates, including the catalytic Tyr residue at position 122 (Tyr-122) and residues whose substitution confers quinolone resistance, notably, Ser-83, Ala-67, Gly-81, Asp-87, Ala-84, and Gln-106. An intragenic region corresponding to 48 amino acids, which is not present in E. coli or other bacteria, was identified in the C-terminal part of A. salmonicida GyrA. This intragenic region shared sequence identity with various DNA-binding proteins of both prokaryotic and eukaryotic origins.

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