The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase

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

Standard

The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase. / Glatt, Sebastian; Létoquart, Juliette; Faux, Céline; Taylor, Nicholas M I; Séraphin, Bertrand; Müller, Christoph W.

In: Nature Structural and Molecular Biology, Vol. 19, No. 3, 2012, p. 314-320.

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

Harvard

Glatt, S, Létoquart, J, Faux, C, Taylor, NMI, Séraphin, B & Müller, CW 2012, 'The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase', Nature Structural and Molecular Biology, vol. 19, no. 3, pp. 314-320. https://doi.org/10.1038/nsmb.2234

APA

Glatt, S., Létoquart, J., Faux, C., Taylor, N. M. I., Séraphin, B., & Müller, C. W. (2012). The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase. Nature Structural and Molecular Biology, 19(3), 314-320. https://doi.org/10.1038/nsmb.2234

Vancouver

Glatt S, Létoquart J, Faux C, Taylor NMI, Séraphin B, Müller CW. The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase. Nature Structural and Molecular Biology. 2012;19(3):314-320. https://doi.org/10.1038/nsmb.2234

Author

Glatt, Sebastian ; Létoquart, Juliette ; Faux, Céline ; Taylor, Nicholas M I ; Séraphin, Bertrand ; Müller, Christoph W. / The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase. In: Nature Structural and Molecular Biology. 2012 ; Vol. 19, No. 3. pp. 314-320.

Bibtex

@article{4f4fd48545284c1592364ea020ec9863,
title = "The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase",
abstract = "Elongator was initially described as an RNA polymerase II-associated factor but has since been associated with a broad range of cellular activities. It has also attracted clinical attention because of its role in certain neurodegenerative diseases. Here we describe the crystal structure of the Saccharomyces cerevisiae subcomplex of Elongator proteins 4, 5 and 6 (Elp456). The subunits each show almost identical RecA folds that form a heterohexameric ring-like structure resembling hexameric RecA-like ATPases. This structural finding is supported by different complementary in vitro and in vivo approaches, including the specific binding of the hexameric Elp456 subcomplex to tRNAs in a manner regulated by ATP. Our results support a role of Elongator in tRNA modification, explain the importance of each of the Elp4, Elp5 and Elp6 subunits for complex integrity and suggest a model for the overall architecture of the holo-Elongator complex.",
keywords = "Models, Molecular, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits/chemistry, RNA, Transfer/chemistry, RNA-Binding Proteins/chemistry, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/chemistry, Substrate Specificity",
author = "Sebastian Glatt and Juliette L{\'e}toquart and C{\'e}line Faux and Taylor, {Nicholas M I} and Bertrand S{\'e}raphin and M{\"u}ller, {Christoph W}",
year = "2012",
doi = "10.1038/nsmb.2234",
language = "English",
volume = "19",
pages = "314--320",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",
number = "3",

}

RIS

TY - JOUR

T1 - The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase

AU - Glatt, Sebastian

AU - Létoquart, Juliette

AU - Faux, Céline

AU - Taylor, Nicholas M I

AU - Séraphin, Bertrand

AU - Müller, Christoph W

PY - 2012

Y1 - 2012

N2 - Elongator was initially described as an RNA polymerase II-associated factor but has since been associated with a broad range of cellular activities. It has also attracted clinical attention because of its role in certain neurodegenerative diseases. Here we describe the crystal structure of the Saccharomyces cerevisiae subcomplex of Elongator proteins 4, 5 and 6 (Elp456). The subunits each show almost identical RecA folds that form a heterohexameric ring-like structure resembling hexameric RecA-like ATPases. This structural finding is supported by different complementary in vitro and in vivo approaches, including the specific binding of the hexameric Elp456 subcomplex to tRNAs in a manner regulated by ATP. Our results support a role of Elongator in tRNA modification, explain the importance of each of the Elp4, Elp5 and Elp6 subunits for complex integrity and suggest a model for the overall architecture of the holo-Elongator complex.

AB - Elongator was initially described as an RNA polymerase II-associated factor but has since been associated with a broad range of cellular activities. It has also attracted clinical attention because of its role in certain neurodegenerative diseases. Here we describe the crystal structure of the Saccharomyces cerevisiae subcomplex of Elongator proteins 4, 5 and 6 (Elp456). The subunits each show almost identical RecA folds that form a heterohexameric ring-like structure resembling hexameric RecA-like ATPases. This structural finding is supported by different complementary in vitro and in vivo approaches, including the specific binding of the hexameric Elp456 subcomplex to tRNAs in a manner regulated by ATP. Our results support a role of Elongator in tRNA modification, explain the importance of each of the Elp4, Elp5 and Elp6 subunits for complex integrity and suggest a model for the overall architecture of the holo-Elongator complex.

KW - Models, Molecular

KW - Protein Binding

KW - Protein Structure, Quaternary

KW - Protein Structure, Tertiary

KW - Protein Subunits/chemistry

KW - RNA, Transfer/chemistry

KW - RNA-Binding Proteins/chemistry

KW - Saccharomyces cerevisiae/enzymology

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Substrate Specificity

U2 - 10.1038/nsmb.2234

DO - 10.1038/nsmb.2234

M3 - Journal article

C2 - 22343726

VL - 19

SP - 314

EP - 320

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 3

ER -

ID: 194521372