title: The R3H domain stabilizes poly(A)-specific ribonuclease by stabilizing the RRM domain.
abstract: Poly(A)-specific ribonuclease (PARN), a key enzyme involved in eukaryotic mRNA decay, contains one catalytic domain and two RNA-binding domains. Here we found that at least one RNA-binding domain is required for the substrate binding, but not for the catalysis of PARN. The removal of the R3H domain led to a dramatic decrease in PARN stability and a change in the aggregation kinetic regime, while only minor effects were observed for the removal of the RRM domain or both RNA-binding domains. Thus the R3H domain might stabilize PARN by acting as a protector or intermolecular chaperone of the RRM domain.
authors.affiliation: State Key Laboratory of Biomembrane and Membrane Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
authors.forename: Wei-Feng
authors.initials: WF
authors.lastname: Liu
authors.forename: Ao
authors.initials: A
authors.lastname: Zhang
authors.forename: Guang-Jun
authors.initials: GJ
authors.lastname: He
authors.forename: Yong-Bin
authors.initials: YB
authors.lastname: Yan
mesh_terms: D001483:Base Sequence; D017931:DNA Primers; D004795:Enzyme Stability; D005095:Exoribonucleases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D009154:Mutation; D013056:Spectrophotometry, Ultraviolet
chemical_list: D017931:DNA Primers; D005095:Exoribonucleases; C024843:poly A specific exoribonuclease