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Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.

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Standard

Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA. / Gromadski, Kirill B; Schümmer, Tobias; Strømgaard, Anne; Knudsen, Charlotte Rohde; Kinzy, Terri Goss; Rodnina, Marina V.

I: Journal of Biological Chemistry, Bind 282, Nr. 49, 2007, s. 35629-37.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Gromadski, KB, Schümmer, T, Strømgaard, A, Knudsen, CR, Kinzy, TG & Rodnina, MV 2007, 'Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.', Journal of Biological Chemistry, bind 282, nr. 49, s. 35629-37. https://doi.org/10.1074/jbc.M707245200

APA

Gromadski, K. B., Schümmer, T., Strømgaard, A., Knudsen, C. R., Kinzy, T. G., & Rodnina, M. V. (2007). Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA. Journal of Biological Chemistry, 282(49), 35629-37. https://doi.org/10.1074/jbc.M707245200

CBE

Gromadski KB, Schümmer T, Strømgaard A, Knudsen CR, Kinzy TG, Rodnina MV. 2007. Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA. Journal of Biological Chemistry. 282(49):35629-37. https://doi.org/10.1074/jbc.M707245200

MLA

Vancouver

Gromadski KB, Schümmer T, Strømgaard A, Knudsen CR, Kinzy TG, Rodnina MV. Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA. Journal of Biological Chemistry. 2007;282(49):35629-37. https://doi.org/10.1074/jbc.M707245200

Author

Gromadski, Kirill B ; Schümmer, Tobias ; Strømgaard, Anne ; Knudsen, Charlotte Rohde ; Kinzy, Terri Goss ; Rodnina, Marina V. / Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA. I: Journal of Biological Chemistry. 2007 ; Bind 282, Nr. 49. s. 35629-37.

Bibtex

@article{7a99a340da4511dcbc43000ea68e967b,
title = "Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.",
abstract = "The interactions of elongation factor 1A (eEF1A) from Saccharomyces cerevisiae with elongation factor 1Balpha (eEF1Balpha), guanine nucleotides, and aminoacyl-tRNA were studied kinetically by fluorescence stopped-flow. eEF1A has similar affinities for GDP and GTP, 0.4 and 1.1 microm, respectively. Dissociation of nucleotides from eEF1A in the absence of the guanine nucleotide exchange factor is slow (about 0.1 s(-1)) and is accelerated by eEF1Balpha by 320-fold and 250-fold for GDP and GTP, respectively. The rate constant of eEF1Balpha binding to eEF1A (10(7)-10(8) M (-1) s(-1)) is independent of guanine nucleotides. At the concentrations of nucleotides and factors prevailing in the cell, the overall exchange rate is expected to be in the range of 6 s(-1), which is compatible with the rate of protein synthesis in the cell. eEF1A.GTP binds Phe-tRNA(Phe) with a K(d) of 3 nm, whereas eEF1A.GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu. Udgivelsesdato: 2007-Dec-7",
keywords = "Guanosine Diphosphate, Guanosine Triphosphate, Kinetics, Peptide Elongation Factor 1, Peptide Elongation Factor Tu, Protein Binding, RNA, Transfer, Amino Acyl, RNA, Transfer, Phe, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins",
author = "Gromadski, {Kirill B} and Tobias Sch{\"u}mmer and Anne Str{\o}mgaard and Knudsen, {Charlotte Rohde} and Kinzy, {Terri Goss} and Rodnina, {Marina V}",
year = "2007",
doi = "10.1074/jbc.M707245200",
language = "English",
volume = "282",
pages = "35629--37",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "49",

}

RIS

TY - JOUR

T1 - Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.

AU - Gromadski, Kirill B

AU - Schümmer, Tobias

AU - Strømgaard, Anne

AU - Knudsen, Charlotte Rohde

AU - Kinzy, Terri Goss

AU - Rodnina, Marina V

PY - 2007

Y1 - 2007

N2 - The interactions of elongation factor 1A (eEF1A) from Saccharomyces cerevisiae with elongation factor 1Balpha (eEF1Balpha), guanine nucleotides, and aminoacyl-tRNA were studied kinetically by fluorescence stopped-flow. eEF1A has similar affinities for GDP and GTP, 0.4 and 1.1 microm, respectively. Dissociation of nucleotides from eEF1A in the absence of the guanine nucleotide exchange factor is slow (about 0.1 s(-1)) and is accelerated by eEF1Balpha by 320-fold and 250-fold for GDP and GTP, respectively. The rate constant of eEF1Balpha binding to eEF1A (10(7)-10(8) M (-1) s(-1)) is independent of guanine nucleotides. At the concentrations of nucleotides and factors prevailing in the cell, the overall exchange rate is expected to be in the range of 6 s(-1), which is compatible with the rate of protein synthesis in the cell. eEF1A.GTP binds Phe-tRNA(Phe) with a K(d) of 3 nm, whereas eEF1A.GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu. Udgivelsesdato: 2007-Dec-7

AB - The interactions of elongation factor 1A (eEF1A) from Saccharomyces cerevisiae with elongation factor 1Balpha (eEF1Balpha), guanine nucleotides, and aminoacyl-tRNA were studied kinetically by fluorescence stopped-flow. eEF1A has similar affinities for GDP and GTP, 0.4 and 1.1 microm, respectively. Dissociation of nucleotides from eEF1A in the absence of the guanine nucleotide exchange factor is slow (about 0.1 s(-1)) and is accelerated by eEF1Balpha by 320-fold and 250-fold for GDP and GTP, respectively. The rate constant of eEF1Balpha binding to eEF1A (10(7)-10(8) M (-1) s(-1)) is independent of guanine nucleotides. At the concentrations of nucleotides and factors prevailing in the cell, the overall exchange rate is expected to be in the range of 6 s(-1), which is compatible with the rate of protein synthesis in the cell. eEF1A.GTP binds Phe-tRNA(Phe) with a K(d) of 3 nm, whereas eEF1A.GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu. Udgivelsesdato: 2007-Dec-7

KW - Guanosine Diphosphate

KW - Guanosine Triphosphate

KW - Kinetics

KW - Peptide Elongation Factor 1

KW - Peptide Elongation Factor Tu

KW - Protein Binding

KW - RNA, Transfer, Amino Acyl

KW - RNA, Transfer, Phe

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

U2 - 10.1074/jbc.M707245200

DO - 10.1074/jbc.M707245200

M3 - Journal article

VL - 282

SP - 35629

EP - 35637

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 49

ER -