The recA gene from the thermophile Thermus aquaticus YT-1: cloning, expression, and characterization
نویسندگان
چکیده
منابع مشابه
amplification and cloning of taq dna polymerase gene from thermus aquaticus strain yt-1
dna amplification using taq dna polymerase is one of the most widely used techniques in molecular biology and biotechnology. the aim of this study was to amplify the gene of this enzyme from a thermophilic bacteria called thermus aqauticus and clone it into a vector for future use. using specific primers the cdna of taq dna polymerase was amplified and ligated into the cloning vector ptz57r usi...
متن کاملCloning and Expression of Thermus Aquaticus DNA Polymerase Gene, Using a Thermo-Inducible Expression Vector
DNA polymerase gene from Thermus aquaticus strain YT1 was amplified using VENTTM DNA po-lymerase and cloned under the control of X.PR promoter and expression was induced by a shift in tern perature. The culture was then sonicated, and after centrifugation the lysate was treated with polyethyleneimine followed by a salting-out step. Finally the protein was precipitated with ammonium sulfate and...
متن کاملPurification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus.
An inorganic pyrophosphatase was purified over 600-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The enzyme is a tetramer of Mr = 84,000, has a sedimentation coefficient of 5.8S, a Stokes radius of 3.5 nm, and an isoelectric point of 5.7. Like the enzyme of Escherichia coli, the pyrophosphatase appears to be made constitutively. The pH and temperature optima are 8.3 and 8...
متن کاملThermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose.
The amylomaltase gene of the thermophilic bacterium Thermus aquaticus ATCC 33923 was cloned and sequenced. The open reading frame of this gene consisted of 1,503 nucleotides and encoded a polypeptide that was 500 amino acids long and had a calculated molecular mass of 57,221 Da. The deduced amino acid sequence of the amylomaltase exhibited a high level of homology with the amino acid sequence o...
متن کاملMolecular cloning and nucleotide sequence of the aminopeptidase T gene of Thermus aquaticus YT-1 and its high-level expression in Escherichia coli.
Aminopeptidase T (AP-T) is a metallo-dependent dimeric enzyme of Thermus aquaticus YT-1, an extremely thermophilic bacterium. We cloned the AP-T gene from T. aquaticus YT-1 into Escherichia coli using a synthetic oligonucleotide as a hybridization probe. The nucleotide sequence of the AP-T gene was found to encode 408 amino acid residues with GTG as a start codon. The molecular weight was calcu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1994
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.176.5.1405-1412.1994