Interaction of mitochondrial elongation factors Tu.Ts with aminoacyl-tRNA.

L. A. Benkowski; C. Takemoto; G. Ott; M. Beikman; T. Ueda; K. Watanabe; M. Sprinzl; L. L. Spremulli

Interaction of mitochondrial elongation factors Tu.Ts with aminoacyl-tRNA.

L. A. Benkowski^*, C. Takemoto, G. Ott, M. Beikman, T. Ueda, K. Watanabe, M. Sprinzl, L. L. Spremulli

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

The interaction between the bovine mitochondrial translational elongation factor Tu.Ts complex (EF-Tu.Tsmt) and aminoacyl-tRNA has been investigated using a nuclease protection assay and fluorescence enhancement of [AEDANS-s2C]Tyr-tRNA(Tyr). The equilibrium dissociation constant, Kd, for the EF-Tu.Tsmt:GTP:E. coli Phe-tRNA complex is approximately 50 nM. A similar binding constant (30 nM) is obtained using bovine mitochondrial Phe-tRNA. The equilibrium binding constant for the EF-Tu.Tsmt:GTP:yeast [AEDANS-s2C]Tyr-tRNA(Tyr) complex is approximately 4 nM when determined using the fluorescence enhancement assay.

Original language	English
Pages (from-to)	163-166
Number of pages	4
Journal	Nucleic acids symposium series
Issue number	33
Publication status	Published - 1995
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

Cite this

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title = "Interaction of mitochondrial elongation factors Tu.Ts with aminoacyl-tRNA.",

abstract = "The interaction between the bovine mitochondrial translational elongation factor Tu.Ts complex (EF-Tu.Tsmt) and aminoacyl-tRNA has been investigated using a nuclease protection assay and fluorescence enhancement of [AEDANS-s2C]Tyr-tRNA(Tyr). The equilibrium dissociation constant, Kd, for the EF-Tu.Tsmt:GTP:E. coli Phe-tRNA complex is approximately 50 nM. A similar binding constant (30 nM) is obtained using bovine mitochondrial Phe-tRNA. The equilibrium binding constant for the EF-Tu.Tsmt:GTP:yeast [AEDANS-s2C]Tyr-tRNA(Tyr) complex is approximately 4 nM when determined using the fluorescence enhancement assay.",

author = "Benkowski, {L. A.} and C. Takemoto and G. Ott and M. Beikman and T. Ueda and K. Watanabe and M. Sprinzl and Spremulli, {L. L.}",

year = "1995",

language = "English",

pages = "163--166",

journal = "Nucleic acids symposium series",

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T1 - Interaction of mitochondrial elongation factors Tu.Ts with aminoacyl-tRNA.

AU - Benkowski, L. A.

AU - Takemoto, C.

AU - Ott, G.

AU - Beikman, M.

AU - Ueda, T.

AU - Watanabe, K.

AU - Sprinzl, M.

AU - Spremulli, L. L.

PY - 1995

Y1 - 1995

N2 - The interaction between the bovine mitochondrial translational elongation factor Tu.Ts complex (EF-Tu.Tsmt) and aminoacyl-tRNA has been investigated using a nuclease protection assay and fluorescence enhancement of [AEDANS-s2C]Tyr-tRNA(Tyr). The equilibrium dissociation constant, Kd, for the EF-Tu.Tsmt:GTP:E. coli Phe-tRNA complex is approximately 50 nM. A similar binding constant (30 nM) is obtained using bovine mitochondrial Phe-tRNA. The equilibrium binding constant for the EF-Tu.Tsmt:GTP:yeast [AEDANS-s2C]Tyr-tRNA(Tyr) complex is approximately 4 nM when determined using the fluorescence enhancement assay.

AB - The interaction between the bovine mitochondrial translational elongation factor Tu.Ts complex (EF-Tu.Tsmt) and aminoacyl-tRNA has been investigated using a nuclease protection assay and fluorescence enhancement of [AEDANS-s2C]Tyr-tRNA(Tyr). The equilibrium dissociation constant, Kd, for the EF-Tu.Tsmt:GTP:E. coli Phe-tRNA complex is approximately 50 nM. A similar binding constant (30 nM) is obtained using bovine mitochondrial Phe-tRNA. The equilibrium binding constant for the EF-Tu.Tsmt:GTP:yeast [AEDANS-s2C]Tyr-tRNA(Tyr) complex is approximately 4 nM when determined using the fluorescence enhancement assay.

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M3 - Article

C2 - 8643359

AN - SCOPUS:0029450011

SN - 0261-3166

SP - 163

EP - 166

JO - Nucleic acids symposium series

JF - Nucleic acids symposium series

IS - 33

ER -

Interaction of mitochondrial elongation factors Tu.Ts with aminoacyl-tRNA.

Abstract

ASJC Scopus subject areas

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