Elongation factor Tu.ribosome dependent GTP hydrolysis: elucidation of the role of the AA-tRNA 3' terminus and site(s) involved in the inducing of the GTPase reaction

Bhuta, Prakash; Kumar, Gyanendra; Chládek, Stanislav

doi:10.1021/bi00534a014

Cited by 26 publications

(13 citation statements)

References 37 publications

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“…What is uncontested the experimental evidence demonstrating the primary importance of the aminoacylated 3' end of aa-tRNA for the stimulation of the GTPase center of EF-Tu [ 11,27,28]. The present work suggests that another, as yet unidentified region of the aa-tRNA * EF-Tu complex, including His"', constrains the GTP-binding site of the protein into a catalytically inactive conformation, if aa-tRNA is present.…”

Section: Discussionsupporting

confidence: 51%

Histidine‐118 of elongation factor Tu: its role in aminoacyl‐tRNA binding and regulation of the GTPase activity

1994

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The function of His"* in elongation factor (EF)-Tu from Escherichia coli was investigated by its substitution with glycine. The substitution had a differential effect on individual functions of the protein. The affinity for aminoacyl (aa)-tRNA and the intrinsic GTPase activity of the mutant EF-Tu were decreased whereas the response of its GTPase center to aa-tRNA was strongly increased. These results suggest that the region around Hisi's is involved in the binding of aa-tRNA and in the transmission of a turn-off signal generated by the interaction with aa-tRNA and directed to the GTPase center of EF-Tu.

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Section: Discussionsupporting

confidence: 51%

Histidine‐118 of elongation factor Tu: its role in aminoacyl‐tRNA binding and regulation of the GTPase activity

1994

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“…The kirromycin-induced GTPase displays many features of the physiological enzyme and is strongly stimulated by ribosomes or tRNA (1,3). Various researchers have utilized this stimulation to study the interaction between EF-Tu and tRNA or fragments thereof (1,(4)(5)(6)(7)(8)(9)(10)(11)(12).…”

mentioning

confidence: 99%

GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site.

Noort¹,

Kraal²,

Bosch³

1986

Proc. Natl. Acad. Sci. U.S.A.

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GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site (GTP February 20, 1986 ABSTRACT Interaction of the elongation factor EF-Tu with the antibiotic kirromycin results in activation of the GTPase center of the factor and in induction of an additional tRNA binding site (tRNA binding site II to distinguish it from the classical tRNA binding site I). Activation of the GTPase center under these conditions is stimulated by addition of tRNA. Two-fold evidence is presented that this stimulation is due to tRNA binding to site II rather than to site I. First, a strong correlation is observed between stimulation of the GTPase activity and enhancement of the reactivity of Cys-81 of EF-Tu toward N-ethylmaleimide at various concentrations of aminoacyl-tRNA, deacylated tRNA, and N-acetylaminoacyltRNA. The latter effects signal tRNA binding to site II. Stimulation of the kirromycin-induced GTPase activity by

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“…Although L-amino acids and some a,a-disubstituted amino acids such as a-aminoisobutyric acid (AIB) and cyclopentylglycine can be incorporated into proteins, D-amino acids do not seem to be accommodated by the translational machinery (58). Interestingly, previous experiments, in which the ability of an ammoacyl-tRNA or aminoacyl-CpA to bind to the E. coli nbosomal A-site and participate in peptide elongation was studied, suggested that achiral amino acids like AIB could not be used as substrates by the E. coli protein biosynthetic machinery (61)(62)(63). Interestingly, previous experiments, in which the ability of an ammoacyl-tRNA or aminoacyl-CpA to bind to the E. coli nbosomal A-site and participate in peptide elongation was studied, suggested that achiral amino acids like AIB could not be used as substrates by the E. coli protein biosynthetic machinery (61)(62)(63).…”

Section: Scope Of the Methodologymentioning

confidence: 99%

Protein Synthesis

Martin¹

1998

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PrefaceThe synthesis of proteins from 20 or so constituent amino acids according to a strictly defined code with an accuracy of better than 1 in 10,000 at most locations is arguably the most complex task performed by cells. Protein Synthesis collects together methods and protocols covering a range of different approaches towards understanding how the cellular machinery accomplishes this task and how these ftinctions might be harnessed by the biotechnology industry to generate novel and useful proteins.The era in which the components of the translational machinery were being catalogued is over. This volume gathers together protocols that focus on preserving and describing the dynamic function as closely as possible. The need to understand exactly how ribosomes are positioned on messages or where tRNA molecules, translation factors, or control proteins are bound, has been appreciated by many of the authors. Several chapters that explore the fidelity and processivity of translation reflect this belief. Moreover, the fundamental importance of rRNA at the heart of the ribosome is a strong theme in a number of the protocols.These articles include in vitro and in vivo systems from bacterial, fungal, plant, and animal systems. Overall, Protein Synthesis might be characterized by the novelty of the approaches employed to illuminate the inner workings of the protein synthetic machinery as well as by the inventiveness of the attempts to harness these reactions for biotechnological applications.Robin Martin

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Elongation factor Tu.ribosome dependent GTP hydrolysis: elucidation of the role of the AA-tRNA 3' terminus and site(s) involved in the inducing of the GTPase reaction

Cited by 26 publications

References 37 publications

Histidine‐118 of elongation factor Tu: its role in aminoacyl‐tRNA binding and regulation of the GTPase activity

Histidine‐118 of elongation factor Tu: its role in aminoacyl‐tRNA binding and regulation of the GTPase activity

GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site.

Protein Synthesis

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