Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 360, Issue 4, Pages 846-851Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2007.06.139
Keywords
domain interactions; poly(A) specific ribonuclease; thermal inactivation; thermal stability; thermal aggregation
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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. (c) 2007 Elsevier Inc. All rights reserved.
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