H, ¹⁵N, ¹³C assignment and secondary structure determination of two domains of La protein from D. discoideum

Biosynthesis of RNA polymerase III transcripts requires binding of the La protein at their 3' end. La is an abundant nuclear RNA-binding protein which protects the nascent transcripts from 3' exonuclease degradation. Here, we report the high yield expression and preliminary structural anal...

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Veröffentlicht in:Biomolecular NMR assignments 2014-04, Vol.8 (1), p.47-51
Hauptverfasser: Apostolidi, Maria, Vourtsis, Dionysios J, Chasapis, Christos T, Stathopoulos, Constantinos, Bentrop, Detlef, Spyroulias, Georgios A
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Sprache:eng
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Zusammenfassung:Biosynthesis of RNA polymerase III transcripts requires binding of the La protein at their 3' end. La is an abundant nuclear RNA-binding protein which protects the nascent transcripts from 3' exonuclease degradation. Here, we report the high yield expression and preliminary structural analysis through NMR spectroscopy of two recombinant RNA binding domains (La motif and NRRM) from the La protein of Dictyostelium discoideum. Both recombinant protein constructs were well-folded and allowed for an almost complete sequence-specific assignment of the (15)N and (13)C labeled domains and their secondary structure prediction using PECAN online tool.
ISSN:1874-270X
DOI:10.1007/s12104-012-9450-6