PMID- 12030365 OWN - NLM STAT- MEDLINE DCOM- 20030206 LR - 20220310 IS - 0300-8177 (Print) IS - 0300-8177 (Linking) VI - 232 IP - 1-2 DP - 2002 Mar TI - Correlation between intrinsic mRNA stability and the affinity of AUF1 (hnRNP D) and HuR for A+U-rich mRNAs. PG - 1-11 AB - Presence of A+U-rich elements (AREs) within 3'-untranslated regions (3'UTRs) of numerous mRNAs has been associated with rapid mRNA turnover; however, the interaction of specific factors with AREs is also associated with mRNA stabilization. Recently, two ARE binding proteins with putative mRNA destabilizing (AUF1) and stabilizing (HuR) properties have been described. However, no direct comparison ofAUF1 and HuR binding properties has been made. Therefore, we examined the relative affinities of p37AUF1 and HuR for a diverse set ofARE-containing mRNAs encoding beta-adrenergic receptors, a proto-oncogene, and a cytokine. We find that high-affinity AUF1 binding appears to require elements beyond primary nucleotide sequence. In contrast, binding of HuR appears considerably less constrained. As a functional correlate, we determined the ability of these specific mRNA sequences to affect the stability of chimeric beta-globin mRNA constructs. Although the relative affinity ofAUF1 and HuR are generally predictive of mRNA stability, we find that certain mRNA sequences do not conform to these generalizations. FAU - Blaxall, Burns C AU - Blaxall BC AD - Department of Pharmacology, University of Colorado Health Sciences Center, Denver 80262, USA. FAU - Pende, Aldo AU - Pende A FAU - Wu, Steven C AU - Wu SC FAU - Port, J David AU - Port JD LA - eng GR - R01 HL051239/HL/NHLBI NIH HHS/United States GR - HL51239/HL/NHLBI NIH HHS/United States GR - GM07635/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S. PL - Netherlands TA - Mol Cell Biochem JT - Molecular and cellular biochemistry JID - 0364456 RN - 0 (3' Untranslated Regions) RN - 0 (Antigens, Surface) RN - 0 (ELAV Proteins) RN - 0 (ELAV-Like Protein 1) RN - 0 (ELAVL1 protein, human) RN - 0 (HNRNPD protein, human) RN - 0 (Heterogeneous Nuclear Ribonucleoprotein D0) RN - 0 (Heterogeneous-Nuclear Ribonucleoprotein D) RN - 0 (MAS1 protein, human) RN - 0 (Proto-Oncogene Mas) RN - 0 (RNA-Binding Proteins) RN - 0 (Recombinant Proteins) RN - 0 (Regulatory Sequences, Ribonucleic Acid) RN - 56HH86ZVCT (Uracil) RN - 9004-22-2 (Globins) RN - JAC85A2161 (Adenine) SB - IM MH - 3' Untranslated Regions/genetics/*metabolism MH - Adenine MH - Animals MH - *Antigens, Surface MH - Base Composition MH - Base Sequence MH - Cricetinae MH - ELAV Proteins MH - ELAV-Like Protein 1 MH - Electrophoretic Mobility Shift Assay MH - Globins/*genetics MH - Half-Life MH - Heterogeneous Nuclear Ribonucleoprotein D0 MH - Heterogeneous-Nuclear Ribonucleoprotein D/*metabolism MH - Humans MH - Protein Binding MH - Proto-Oncogene Mas MH - *RNA Stability MH - RNA-Binding Proteins/*metabolism MH - Recombinant Proteins/metabolism MH - Regulatory Sequences, Ribonucleic Acid/genetics MH - Time Factors MH - Transfection MH - Ultraviolet Rays MH - Uracil EDAT- 2002/05/28 10:00 MHDA- 2003/02/07 04:00 CRDT- 2002/05/28 10:00 PHST- 2002/05/28 10:00 [pubmed] PHST- 2003/02/07 04:00 [medline] PHST- 2002/05/28 10:00 [entrez] AID - 10.1023/a:1014819016552 [doi] PST - ppublish SO - Mol Cell Biochem. 2002 Mar;232(1-2):1-11. doi: 10.1023/a:1014819016552.