The kinetic mechanism of the release of nucleotide from elongation factor Tu promoted by elongation factor Ts determined by pressure relaxation studies.
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...
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دوره مشترک کارشناسی ارشد بازاریابی و تجارت الکترونیک دانشگاه تربیت مدرس_ دانشگاه تکنولوژی lule? چکیده پایان نامه عوامل موثر بر پذیرش اینترنت بانک توسط مشتریان پیشرفت فناوری اطلاعات و ارتباطات و به طور خاص رشد اینترنت جهت تراکنش های معاملات بازرگانی، تاثیر بسیار عمیقی در صنعت بانکداری داشته است.این در حالی ست که نفوذ بانکداری اینترنتی در کشورهای در حال توسعه بسیار کندتر از نفوذ آن ...
15 صفحه اولInteraction 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 کاملMechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base.
Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Similarly to other GTP-binding proteins, the structural changes in the P loop and the Mg(2+) binding site are known to be important for nucleotide release from EF-Tu. In the present paper, we determine the contribution of the contacts between helix D of EF-Tu at the base side of the nucleotide and ...
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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)68834-9