| Range |
Table - link
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Chen JF, Guo NN, Li T, Wang ED, Wang YL. CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function. Biochemistry. 2000 Jun 6 39(22):6726-31.PubMed ID10828991
|
| Method |
Construction of a Plasmid Containing the Gene Encoding
His6-Tagged LeuRS-B. Cloning and Expression of the Gene Encoding CP1Leu. Assay of Enzyme ActiVity. Circular Dichroism (CD) Spectroscopy. |
| Comments |
Aminoacyl-tRNA synthetases (aaRSs)1 arose early in
evolution and are believed to be a group of ancient enzymes
that catalyze the precise charging of tRNAs with their
cognate amino acids (1). The aminoacylation of tRNA is a
two-step reaction: (a) activation of amino acids with ATP
by forming aminoacyl adenylates and (b) transferring of the
aminoacyl residue from the aminoacyl adenylate to the
cognate tRNA substrate (2). The accuracy of aminoacylation
depends on both the specific recognition of amino acids
during their activations (coarse sieve) and the pre- or posttransferring
editing (fine sieve) that correct errors at either
the aminoacyl adenylate level or the tRNA level. |
| Entered by |
Uri M |
| ID |
104980 |