2lu0

Publication Abstract from PubMed

Folding of group II introns is characterized by a first slow compaction of domain 1 (D1) followed by the rapid docking of other domains to this scaffold. D1 compaction initiates in a small subregion encompassing the kappa and zeta elements. These two tertiary elements are also the major interaction sites with domain 5 to form the catalytic core. Here, we provide the first characterization of the structure adopted at an early folding step and show that the folding control element can be narrowed down to the three-way junction with the kappa motif. In our nuclear magnetic resonance studies of this substructure derived from the yeast mitochondrial group II intron Sc.ai5gamma, we show that a high affinity Mg(II) ion stabilizes the kappa element and enables coaxial stacking between helices d' and d, favoring a rigid duplex across the three-way junction. The kappa-element folds into a stable GAAA-tetraloop motif and engages in A-minor interactions with helix d'. The addition of cobalt(III)hexammine reveals three distinct binding sites. The Mg(II)-promoted structural rearrangement and rigidification of the D1 core can be identified as the first micro-step of D1 folding.

The structural stabilization of the kappa three-way junction by Mg(II) represents the first step in the folding of a group II intron.,Donghi D, Pechlaner M, Finazzo C, Knobloch B, Sigel RK Nucleic Acids Res. 2013 Feb 1;41(4):2489-504. doi: 10.1093/nar/gks1179. Epub 2012, Dec 28. PMID:23275550^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.