Publication details

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

HOLUB Peter LALÁKOVÁ Jana ČERNÁ Hana PASULKA Josef SÁRAZOVÁ Marie HRAZDILOVÁ Kristýna SAŇUDO ARCE Maria HÓBOR Fruzsina ŠTEFL Richard VAŇÁČOVÁ Štěpánka

Year of publication 2012
Type Article in Periodical
Magazine / Source Nucleic Acids Research
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://nar.oxfordjournals.org/content/early/2012/03/08/nar.gks223.abstract
Doi http://dx.doi.org/10.1093/nar/gks223
Field Genetics and molecular biology
Keywords RNA recognition; binding; RNA processing; RNA-protein interaction
Attached files
Description 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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