Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator

Research output: Contribution to journal › Journal article › Research › peer-review

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Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator. / Petrakis, Thodoris G.; Wittschieben, Birgitte; Svejstrup, Jesper Q.

In: Journal of Biological Chemistry, Vol. 279, No. 31, 30.07.2004, p. 32087-32092.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Petrakis, TG, Wittschieben, B & Svejstrup, JQ 2004, 'Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator', Journal of Biological Chemistry, vol. 279, no. 31, pp. 32087-32092. https://doi.org/10.1074/jbc.M403361200

APA

Petrakis, T. G., Wittschieben, B., & Svejstrup, J. Q. (2004). Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator. Journal of Biological Chemistry, 279(31), 32087-32092. https://doi.org/10.1074/jbc.M403361200

Vancouver

Petrakis TG, Wittschieben B, Svejstrup JQ. Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator. Journal of Biological Chemistry. 2004 Jul 30;279(31):32087-32092. https://doi.org/10.1074/jbc.M403361200

Author

Petrakis, Thodoris G. ; Wittschieben, Birgitte ; Svejstrup, Jesper Q. / Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 31. pp. 32087-32092.

Bibtex

@article{419a0ebf762d4e1cb3c6cbb6f337a47f,
title = "Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator",
abstract = "The molecular architecture of six-subunit yeast holo-Elongator complex was investigated by the use of immunoprecipitation, two-hybrid interaction mapping, and in vitro studies of binary interactions between individual subunits. Surprisingly, Elp2 is dispensable for the integrity of the holo-Elongator complex, and a purified five-subunit elp2Δ Elongator complex retains histone acetyltransferase activity in vitro. These results indicate that the WD40 repeats in Elp2 are required neither for subunit-subunit interactions within Elongator nor for Elongator interaction with histones during catalysis. Elp2 and Elp4 were largely dispensable for the association of Elongator with nascent RNA transcript in vivo. In contrast, Elongator-RNA interaction requires the Elp3 protein. Together, these data shed light on the structure-function relationship of the Elongator complex.",
author = "Petrakis, {Thodoris G.} and Birgitte Wittschieben and Svejstrup, {Jesper Q.}",
year = "2004",
month = jul,
day = "30",
doi = "10.1074/jbc.M403361200",
language = "English",
volume = "279",
pages = "32087--32092",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "31",

}

RIS

TY - JOUR

T1 - Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-Elongator

AU - Petrakis, Thodoris G.

AU - Wittschieben, Birgitte

AU - Svejstrup, Jesper Q.

PY - 2004/7/30

Y1 - 2004/7/30

N2 - The molecular architecture of six-subunit yeast holo-Elongator complex was investigated by the use of immunoprecipitation, two-hybrid interaction mapping, and in vitro studies of binary interactions between individual subunits. Surprisingly, Elp2 is dispensable for the integrity of the holo-Elongator complex, and a purified five-subunit elp2Δ Elongator complex retains histone acetyltransferase activity in vitro. These results indicate that the WD40 repeats in Elp2 are required neither for subunit-subunit interactions within Elongator nor for Elongator interaction with histones during catalysis. Elp2 and Elp4 were largely dispensable for the association of Elongator with nascent RNA transcript in vivo. In contrast, Elongator-RNA interaction requires the Elp3 protein. Together, these data shed light on the structure-function relationship of the Elongator complex.

AB - The molecular architecture of six-subunit yeast holo-Elongator complex was investigated by the use of immunoprecipitation, two-hybrid interaction mapping, and in vitro studies of binary interactions between individual subunits. Surprisingly, Elp2 is dispensable for the integrity of the holo-Elongator complex, and a purified five-subunit elp2Δ Elongator complex retains histone acetyltransferase activity in vitro. These results indicate that the WD40 repeats in Elp2 are required neither for subunit-subunit interactions within Elongator nor for Elongator interaction with histones during catalysis. Elp2 and Elp4 were largely dispensable for the association of Elongator with nascent RNA transcript in vivo. In contrast, Elongator-RNA interaction requires the Elp3 protein. Together, these data shed light on the structure-function relationship of the Elongator complex.

U2 - 10.1074/jbc.M403361200

DO - 10.1074/jbc.M403361200

M3 - Journal article

C2 - 15138274

AN - SCOPUS:3543038157

VL - 279

SP - 32087

EP - 32092

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -

ID: 331040658