AU-rich RNA-binding induces changes in the quaternary structure of AUH.

摘要: The human AU RNA binding protein/enoyl-Coenzyme A hydratase (AUH) is a 3-hydroxy-3-methylglutaconyl-CoA dehydratase in the leucine degradation pathway. It also possesses an RNA-binding activity to AUUU repeats, which involves no known conserved domains and seemingly unrelated enzymatic activity. In this study, we performed mass spectrometric analyses elucidate oligomeric states of AUH presence absence RNA. With short (AUUU) or without RNA, mainly exists as trimer solution. On other hand, dimerizes upon one molecule long containing 24 repeats motif, (AUUU)24A. was crystallized with Although disordered crystalline lattice, structure determined asymmetric dimer trimers kink alignment axes, resulting formation two clefts significantly different sizes. Proteins 2009. © 2008 Wiley-Liss, Inc.