@inbook{fba4edbb6009449fb6044ca1f3f679d9,
title = "Structure and Activities of the Eukaryotic RNA Exosome",
abstract = "The composition of the multisubunit eukaryotic RNA exosome was described more than a decade ago, and structural studies conducted since that time have contributed to our mechanistic understanding of factors that are required for 3'-to-5' RNA processing and decay. This chapter describes the organization of the eukaryotic RNA exosome with a focus on presenting results related to the noncatalytic nine-subunit exosome core as well as the hydrolytic exo- and endoribonuclease Rrp44 (Dis3) and the exoribonuclease Rrp6. This is achieved in large part by describing crystal structures of Rrp44, Rrp6, and the nine-subunit exosome core with an emphasis on how these molecules interact to endow the RNA exosome with its catalytic activities.",
keywords = "3'-to-5' RNA decay, Cold-shock domain, Endoribonuclease, Exoribonuclease, Exosome, Hydrolytic, KH domain, Multisubunit, PH domain, PIN domain, Phosphorolytic, RNA binding, RNA degradation, RNA processing, RNase, S1 domain, Structure",
author = "Wasmuth, \{Elizabeth V.\} and Lima, \{Christopher D.\}",
note = "Funding Information: Research reported in this publication was supported by the National Institute of General Medical Sciences of the National Institutes of Health under award numbers F31GM097910 (E.V.W) and R01GM079196 (C.D.L). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.",
year = "2012",
doi = "10.1016/B978-0-12-404740-2.00003-3",
language = "English (US)",
series = "Enzymes",
publisher = "Academic Press",
pages = "53--75",
booktitle = "Enzymes",
}