Bacterial elongation factor Ts: isolation and reactivity with elongation factor Tu
نویسندگان
چکیده
منابع مشابه
Interaction of mitochondrial elongation factor Tu with aminoacyl-tRNA and elongation factor Ts.
Elongation factor (EF) Tu promotes the binding of aminoacyl-tRNA (aa-tRNA) to the acceptor site of the ribosome. This process requires the formation of a ternary complex (EF-Tu.GTP.aa-tRNA). EF-Tu is released from the ribosome as an EF-Tu.GDP complex. Exchange of GDP for GTP is carried out through the formation of a complex with EF-Ts (EF-Tu.Ts). Mammalian mitochondrial EF-Tu (EF-Tu(mt)) differ...
متن کاملRole of domains in Escherichia coli and mammalian mitochondrial elongation factor Ts in the interaction with elongation factor Tu.
Bovine mitochondrial elongation factor Ts (EF-Tsmt) stimulates the activity of Escherichia coli elongation factor Tu (EF-Tu). In contrast, E. coli EF-Ts is unable to stimulate mitochondrial EF-Tu. EF-Tsmt forms a tight complex with E. coli EF-Tu governed by an association constant of 8.6 x 10(10). This value is 100-fold stronger than the binding constant for the formation of the E. coli EF-Tu.T...
متن کاملThe identification of a domain in Escherichia coli elongation factor Tu that interacts with elongation factor Ts.
A method has been developed to search for the elongation factor Tu (EF-Tu) domain(s) that interact with elongation factor Ts (EF-Ts). This method is based on the suppression of Escherichia coli EF-Tu-dominant negative mutation K136E, a mutation that exerts its effect by sequestering EF-Ts. We have identified nine single-amino acid- substituted suppression mutations in the region 146-199 of EF-T...
متن کاملInteraction 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 کاملSer-tRNAs from bovine mitochondrion form ternary complexes with bacterial elongation factor Tu and GTP.
Transfer ribonucleic acids were isolated from mitochondria of bovine heart and aminoacylated in vitro by a crude mitochondrial enzyme. Ser-tRNASerUCN and Ser-tRNASerAGY were isolated and characterized by partial sequencing. Although these tRNAs possess unique structural features not found in any bacterial tRNA, they form a ternary complex with elongation factor from the extreme thermophilic bac...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1983
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.153.3.1266-1271.1983