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Three Residues Make an Evolutionary Switch for Folding and RNA-Destabilizing Activity in the TTP Family of Proteins.

ACS Chem. Biol.. 2016; 
DeveauLaura M,MassiFranc
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Mutagenesis Services The RBD of human TTP (residues 102-170) and TIS11d (residues 152-220) was synthesized by Genscript and cloned into the pet21b vector between Nde1 and Xho1 restriction sites. Chimeras of TTP and TIS11d were generated via Quikchange mutagenesis.  Get A Quote

摘要

Tristetraprolin (TTP) binds to mRNA transcripts to promote their degradation. The TTP protein family in humans includes two other proteins, TIS11b and TIS11d. All three proteins contain a highly homologous RNA binding domain (RBD) that consists of two CCCH zinc fingers (ZFs). Both ZFs are folded in the absence of RNA in TIS11d and TIS11b. In TTP, however, only ZF1 adopts a stable fold. The focus of this study is to understand the origin and biological significance of the structural differences of the RBD. We identified three residues that affect the affinity for the structural Zn(2+) and determine the folding of ZF2 in the absence of RNA. We observed that the mRNA destabilizing activity of TTP was increas... More

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