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Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation

Basic information
Original title:Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation
Authors:Peter Holub, Jana Laláková, Hana Černá, Josef Pasulka, Marie Sárazová, Kristýna Hrazdilová, Maria Saňudo Arce, Fruzsina Hóbor, Richard Štefl, Štěpánka Vaňáčová
Further information
Citation:HOLUB, Peter, Jana LALÁKOVÁ, Hana ČERNÁ, Josef PASULKA, Marie SÁRAZOVÁ, Kristýna HRAZDILOVÁ, Maria SAŇUDO ARCE, Fruzsina HÓBOR, Richard ŠTEFL and Štěpánka VAŇÁČOVÁ. Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation. Nucleic Acids Research, Oxford: Oxford University Press, 2012, vol. 40, No 12, p. 5679-5693. ISSN 0305-1048. doi:10.1093/nar/gks223.Export BibTeX
@article{982490,
author = {Holub, Peter and Laláková, Jana and Černá, Hana and Pasulka, Josef and Sárazová, Marie and Hrazdilová, Kristýna and Saňudo Arce, Maria and Hóbor, Fruzsina and Štefl, Richard and Vaňáčová, Štěpánka},
article_location = {Oxford},
article_number = {12},
doi = {http://dx.doi.org/10.1093/nar/gks223},
keywords = {RNA recognition; binding; RNA processing; RNA-protein interaction},
language = {eng},
issn = {0305-1048},
journal = {Nucleic Acids Research},
title = {Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation},
url = {http://nar.oxfordjournals.org/content/early/2012/03/08/nar.gks223.abstract},
volume = {40},
year = {2012}
}
Original language:English
Field:Genetics and molecular biology
WWW:link to a new windowhttp://nar.oxfordjournals.org/content/early/2012/03/08/nar.gks223.abstract
Type:Article in Periodical
Keywords:RNA recognition; binding; RNA processing; RNA-protein interaction

Trf4/5p-Air1/2p-Mtr4p polyadenylation complex (TRAMP) is an essential component of nuclear RNA surveillance in yeast. It recognizes a variety of nuclear transcripts produced by all three RNA polymerases, adds short poly(A) tails to aberrant or unstable RNAs and activates the exosome for their degradation. Despite the advances in understanding the structural features of the isolated complex subunits or their fragments, the details of complex assembly, RNA recognition and exosome activation remain poorly understood. Here we provide the first understanding of the RNA binding mode of the complex. We show that Air2p is an RNA-binding subunit of TRAMP. We identify the zinc knuckles (ZnK) 2, 3 and 4 as the RNA-binding domains, and reveal the essentiality of ZnK4 for TRAMP4 polyadenylation activity. Furthermore, we identify Air2p as the key component of TRAMP4 assembly providing bridging between Mtr4p and Trf4p. The former is bound via the N-terminus of Air2p, while the latter is bound via ZnK5, the linker between ZnK4 and 5 and the C-terminus of the protein. Finally, we uncover the RNA binding part of the Mtr4p arch, the KOW domain, as the essential component for TRAMP-mediated exosome activation.

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