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  The Molecular Architecture of the TRAMP Complex Reveals the Organization and Interplay of Its Two Catalytic Activities

Falk, S., Weir, J. R., Hentschel, J., Reichelt, P., Bonneau, F., & Conti, E. (2014). The Molecular Architecture of the TRAMP Complex Reveals the Organization and Interplay of Its Two Catalytic Activities. MOLECULAR CELL, 55(6), 856-867. doi:10.1016/j.molcel.2014.07.020.

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 Creators:
Falk, Sebastian1, Author              
Weir, John R.1, Author              
Hentschel, Jendrik1, Author              
Reichelt, Peter1, Author              
Bonneau, Fabien1, Author              
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: NUCLEAR-RNA SURVEILLANCE; SACCHAROMYCES-CEREVISIAE; QUALITY-CONTROL; CRYSTAL-STRUCTURE; QUANTITATIVE PROTEOMICS; PROTEIN INTERACTIONS; POLY(A) POLYMERASE; RIBOSOMAL-RNA; EXOSOME; DOMAIN
 Abstract: The TRAMP complex is involved in the nuclear surveillance and turnover of noncoding RNAs and intergenic transcripts. TRAMP is associated with the nuclear exosome and consists of a poly(A) polymerase subcomplex (Trf4-Air2) and a helicase (Mtr4). We found that N-terminal low-complexity regions of Trf4 and Air2 bind Mtr4 in a cooperative manner. The 2.4 angstrom resolution crystal structure of the corresponding ternary complex reveals how Trf4 and Air2 wrap around the DExH core of the helicase. Structure-based mutations on the DExH core impair binding to Trf4 and Air2, and also to Trf5 and Air1. The combination of structural, biochemical, and biophysical data suggests that the poly(A) polymerase core of Trf4-Air2 is positioned below the base of the helicase, where the unwound 3 ' end of an RNA substrate is expected to emerge. The results reveal conceptual similarities between the two major regulators of the exosome, the nuclear TRAMP and cytoplasmic Ski complexes.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: MOLECULAR CELL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 55 (6) Sequence Number: - Start / End Page: 856 - 867 Identifier: ISSN: 1097-2765