Site-Directed Mutagenesis of Thermus thermophilus Elongation Factor Tu
نویسندگان
چکیده
منابع مشابه
Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.
The middle and C-terminal domain (domain II/III) of elongation factor Tu from Thermus thermophilus lacking the GTP/GDP binding domain have been prepared by treating nucleotide-free protein with Staphylococcus aureus V8 protease. The isolated domain II/III of EF-Tu has a compact structure and high resistance against tryptic treatment and thermal denaturation. As demonstrated by circular dichrois...
متن کاملThe tRNA specificity of Thermus thermophilus EF-Tu.
By introducing a GAC anticodon, 21 different Escherichia coli tRNAs were misacylated with either phenylalanine or valine and assayed for their affinity to Thermus thermophilus elongation factor Tu (EF-Tu)*GTP by using a ribonuclease protection assay. The presence of a common esterified amino acid permits the thermodynamic contribution of each tRNA body to the overall affinity to be evaluated. T...
متن کاملSite-Directed Mutagenesis in Human Granulocyte-colony Stimulating Factor, Cloning and Expression in Escherichia coli
Human granulocyte colony stimulating factor (hG-CSF) induces proliferation and differentiation of granulocyte progenitor cells. This glycoprotein is currently being used for treatment of neutropenia, in patients who have undergone bone marrow transplantation. So far, different researchers have tried to enhance hG-CSF biological activity and stability. In this study, Polymerase Chain Reaction (P...
متن کاملThe crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
BACKGROUND Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS The crystal structure of EF-Tu from Thermus aquaticus, complexe...
متن کاملSite-Directed Mutagenesis Study
Structural elements of the rat 1.t-opioid receptor important in ligand receptor binding and selectivity were examined using a site-directed mutagenesis approach. Five single amino acid mutations were made, three that altered conserved residues in the ~ 8, and K receptors (Asn 15°t Ala, His297 to Ala, and Tyr326 to Phe) and wo de igned to test for ~i/8 selectivity (lie198 to Val and Va1202 to li...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2008
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1995.0596j.x