scholarly journals DNA Sequence Analysis of a Bioluminescent Marine Bacterium

2008 ◽  
Author(s):  
Benjamin Ryder
Keyword(s):  
Sequence Analysis ◽  
Dna Sequence ◽  
Marine Bacterium ◽  
Dna Sequence Analysis ◽  
Open Reading Frames ◽  
Pha Synthase ◽  
Putative Gene ◽  
Dna Fragment ◽  
Reading Frames

<p>Studies the sequencing of the DNA fragment containing the gene phaC (PHA synthase) and undertakes the search for open reading frames and putative gene matches in a bioluminescent marine bacterium.</p>

XV. Yeast sequencing reports. DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames

Yeast ◽  
1995 ◽  
Vol 11 (13) ◽  
pp. 1281-1288 ◽  
Author(s):  
Antonio Casamayor ◽  
Martí Aldea ◽  
Celia Casas ◽  
Enrique Herrero ◽  
Francisco-Javier Gamo ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Dna Sequence ◽  
Dna Sequence Analysis ◽  
Open Reading Frames ◽  
Yeast Chromosome ◽  
Reading Frames

DNA Sequence Analysis of a 23 002 bp DNA Fragment of the Right Arm ofSaccharomyces cerevisiae Chromosome VII

Yeast ◽  
1997 ◽  
Vol 13 (4) ◽  
pp. 357-363 ◽  
Author(s):  
JAVIER ARROYO ◽  
MELBA GARCÍA-GONZALEZ ◽  
M. ISABEL GARCÍA-SAEZ ◽  
MIGUEL SANCHEZ ◽  
CÉSAR NOMBELA
Keyword(s):  
Sequence Analysis ◽  
Dna Sequence ◽  
Dna Sequence Analysis ◽  
Dna Fragment ◽  
The Right

scholarly journals Cloning and Characterization of a New Site-Specific Methyl-Directed ElmI Endonuclease Recognizing and Cleaving C5-methylated DNA Sequence 5’-G(5mC)^NG(5mC)-3’

Acta Naturae ◽  
2016 ◽  
Vol 8 (1) ◽  
pp. 117-125 ◽  
Author(s):  
V. A. Chernukhin ◽  
D. A. Gonchar ◽  
M. A. Abdurashitov ◽  
O. A. Belichenko ◽  
V. S. Dedkov ◽  
...  
Keyword(s):  
Dna Sequence ◽  
Amino Acid Sequences ◽  
Open Reading Frames ◽  
Site Specific ◽  
Pcr Screening ◽  
Methylated Dna ◽  
Chromatographic Techniques ◽  
Dna Fragment ◽  
Reading Frames

Putative open reading frames of MD-endonucleases have been identified in Enterobacteria genomes as a result of the search for amino acid sequences homologous to MD-endonuclease BisI. A highly conserved DNA primary structure of these open reading frames in different genera of Enterobacteria (Escherichia, Klebsiella and Cronobacter) has allowed researchers to create primers for PCR screening, which was carried out on Enterobacteria DNA collected from natural sources. The DNA fragment, about 440 bp in length, was amplified by use of the genomic DNA of a wild E.coli LM N17 strain as a template and was inserted into the pMTL22 vector. Endonuclease activity was detected in an E.coli ER 2267 strain transformed with the obtained construction. A new enzyme named ElmI was purified by chromatographic techniques from the recombinant strain biomass. It was discovered that similarly to BisI this enzyme specifically cleaves the methylated DNA sequence 5-GCNGC- 3 before the central nucleotide N if this sequence contains two 5-methylcytosines. However, unlike BisI, ElmI more efficiently cleaves this sequence if more than two cytosine residues are methylated.

Sequence Analysis of a 10·5 kb DNA Fragment from the Yeast Chromosome VII Reveals the Presence of Three New Open Reading Frames and of a tRNAThr Gene

Yeast ◽  
1997 ◽  
Vol 13 (4) ◽  
pp. 369-372 ◽  
Author(s):  
CRISTINA MAZZONI ◽  
MAURIZIO RUZZI ◽  
TERESA RINALDI ◽  
FRANCESCA SOLINAS ◽  
FABIOLA MONTEBOVE ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Open Reading Frames ◽  
Yeast Chromosome ◽  
Dna Fragment ◽  
Reading Frames

scholarly journals Mu-Like Prophage in Serogroup B Neisseria meningitidis Coding for Surface-Exposed Antigens

2001 ◽  
Vol 69 (4) ◽  
pp. 2580-2588 ◽  
Author(s):  
Vega Masignani ◽  
Marzia Monica Giuliani ◽  
Hervé Tettelin ◽  
Maurizio Comanducci ◽  
Rino Rappuoli ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Sequence Analysis ◽  
Haemophilus Influenzae ◽  
Neisseria Meningitidis ◽  
Horizontal Transfer ◽  
Open Reading Frames ◽  
Putative Gene ◽  
Nucleotide Content ◽  
Gene Coding ◽  
Reading Frames

ABSTRACT Sequence analysis of the genome of Neisseria meningititdis serogroup B revealed the presence of an ∼35-kb region inserted within a putative gene coding for an ABC-type transporter. The region contains 46 open reading frames, 29 of which are colinear and homologous to the genes of Escherichia coli Mu phage. Two prophages with similar organizations were also found in serogroup A meningococcus, and one was found inHaemophilus influenzae. Early and late phage functions are well preserved in this family of Mu-like prophages. Several regions of atypical nucleotide content were identified. These likely represent genes acquired by horizontal transfer. Three of the acquired genes are shown to code for surface-associated antigens, and the encoded proteins are able to induce bactericidal antibodies.

scholarly journals Molecular Cloning and Heterologous Expression of a Biosynthetic Gene Cluster for the Antitubercular Agent d-Cycloserine Produced by Streptomyces lavendulae

2010 ◽  
Vol 54 (3) ◽  
pp. 1132-1139 ◽  
Author(s):  
Takanori Kumagai ◽  
Yusuke Koyama ◽  
Kosuke Oda ◽  
Masafumi Noda ◽  
Yasuyuki Matoba ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Gene Cluster ◽  
Open Reading Frames ◽  
Strain Atcc ◽  
Biosynthetic Gene ◽  
Putative Gene ◽  
Streptomyces Lavendulae ◽  
Fold Family ◽  
Dna Fragment ◽  
Reading Frames

ABSTRACT In the present study, we successfully cloned a 21-kb DNA fragment containing a d-cycloserine (DCS) biosynthetic gene cluster from a DCS-producing Streptomyces lavendulae strain, ATCC 11924. The putative gene cluster consists of 10 open reading frames (ORFs), designated dcsA to dcsJ. This cluster includes two ORFs encoding d-alanyl-d-alanine ligase (dcsI) and a putative membrane protein (dcsJ) as the self-resistance determinants of the producer organism, indicated by our previous work. When the 10 ORFs were introduced into DCS-nonproducing Streptomyces lividans 66 as a heterologous host cell, the transformant acquired DCS productivity. This reveals that the introduced genes are responsible for the biosynthesis of DCS. As anticipated, the disruption of dcsG, seen in the DCS biosynthetic gene cluster, made it possible for the strain ATCC 11924 to lose its DCS production. We here propose the DCS biosynthetic pathway. First, l-serine is O acetylated by a dcsE-encoded enzyme homologous to homoserine O-acetyltransferase. Second, O-acetyl-l-serine accepts hydroxyurea via an O-acetylserine sulfhydrylase homolog (dcsD product) and forms O-ureido-l-serine. The hydroxyurea must be supplied by the catalysis of a dcsB-encoded arginase homolog using the l-arginine derivative, N G-hydroxy-l-arginine. The resulting O-ureido-l-serine is then racemized to O-ureido-d-serine by a homolog of diaminopimelate epimerase. Finally, O-ureido-d-serine is cyclized to form DCS with the release of ammonia and carbon dioxide. The cyclization must be done by the dcsG or dcsH product, which belongs to the ATP-grasp fold family of protein.

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