کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2029627 1070930 2016 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif
چکیده انگلیسی


• The RBM10 octamer repeat (OCRE) sequence motif is part of a stable globular domain
• 16 aromatic residues result in a unique architecture and surface-exposed tyrosines
• The OCRE globular domain is conserved across the animal kingdom in RBM10 and RBM5

SummaryThe OCtamer REpeat (OCRE) has been annotated as a 42-residue sequence motif with 12 tyrosine residues in the spliceosome trans-regulatory elements RBM5 and RBM10 (RBM [RNA-binding motif]), which are known to regulate alternative splicing of Fas and Bcl-x pre-mRNA transcripts. Nuclear magnetic resonance structure determination showed that the RBM10 OCRE sequence motif is part of a 55-residue globular domain containing 16 aromatic amino acids, which consists of an anti-parallel arrangement of six β strands, with the first five strands containing complete or incomplete Tyr triplets. This OCRE globular domain is a distinctive component of RBM10 and is more widely conserved in RBM10s across the animal kingdom than the ubiquitous RNA recognition components. It is also found in the functionally related RBM5. Thus, it appears that the three-dimensional structure of the globular OCRE domain, rather than the 42-residue OCRE sequence motif alone, confers specificity on RBM10 intermolecular interactions in the spliceosome.

Graphical AbstractFigure optionsDownload high-quality image (145 K)Download as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 24, Issue 1, 5 January 2016, Pages 158–164
نویسندگان
, , , ,