Isolation and purification isoaccepting tRNA1Ser and tRNA2Ser from Thermus thermophilus
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چکیده
منابع مشابه
Cloning, purification and crystallization of Thermus thermophilus proline dehydrogenase.
Nature recycles L-proline by converting it to L-glutamate. This four-electron oxidation process is catalyzed by the two enzymes: proline dehydrogenase (PRODH) and Delta1-pyrroline-5-carboxylate dehydrogenase. This note reports the cloning, purification and crystallization of Thermus thermophilus PRODH, which is the prototype of a newly discovered superfamily of bacterial monofunctional PRODHs. ...
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A recJ homolog was cloned from the extremely thermophilic bacterium Thermus themophilus HB8. It encodes a 527 amino acid protein that has 33% identity to Escherichia coli RecJ protein and includes the characteristic motifs conserved among RecJ homologs. Although T.thermophilus RecJ protein (ttRecJ) was expressed as an inclusion body, it was purified in soluble form through denaturation with ure...
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Thermus thermophilus ribonuclease H was overexpressed and purified from Escherichia coli. The determination of the complete amino acid sequence allowed modification of that predicted from the DNA sequence, and the enzyme was shown to be composed of 166 amino acid residues with a molecular weight of 18,279. The isoelectric point of the enzyme was 10.5, and the specific absorption coefficient A0....
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We describe the crystallization and structure determination of the 30 S ribosomal subunit from Thermus thermophilus. Previous reports of crystals that diffracted to 10 A resolution were used as a starting point to improve the quality of the diffraction. Eventually, ideas such as the addition of substrates or factors to eliminate conformational heterogeneity proved less important than attention ...
متن کاملPurification and initial characterization of RNA polymerase from Thermus thermophilus strain HB8.
Utilizing a novel and rapid two-column purification procedure, the DNA-dependent RNA polymerase (RNAP) from the thermophile, Thermus thermophilus HB8, was purified to electrophoretic homogeneity with a recovery of 65% (as determined by RNAP activity) in less than 2 days. The purified enzyme was characterized using DNA containing the lambdaP(R) promoter. KMnO(4) footprinting, abortive initiation...
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 2006
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.000748