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Interaction properties of human TRAMP‐like proteins and their role in pre‐rRNA 5′ETS turnover
Author(s) -
Sudo Haruka,
Nozaki Aya,
Uno Hideaki,
Ishida Yoichi,
Nagahama Masami
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12314
Subject(s) - tramp , exosome complex , microbiology and biotechnology , rna , ribosomal rna , exosome , protein subunit , polyadenylation , chemistry , biology , biochemistry , microvesicles , gene , non coding rna , microrna , transgene
In yeast, the Trf4/5‐Air1/2‐Mtr4 polyadenylation (TRAMP) complex acts as a cofactor for the nuclear exosome to promote degradation of various RNAs. However, the corresponding machinery in mammals is less characterized. We analyzed the interactions of the human TRAMP‐like proteins, PAPD5, ZCCHC7, and MTR4, with the nuclear exosome. PAPD5 and ZCCHC7 exhibited mutual interactions in presence of the exosome catalytic subunit RRP6, whereas MTR4 was dispensable for their assembly. Furthermore, the human TRAMP‐like proteins were involved in the RRP6‐catalyzed turnover of pre‐rRNA 5′ETS fragments. These results suggest the significant role for RRP6 in the assembly of TRAMP‐like proteins during nucleolar RNA surveillance.