Purification by affinity chromatography of H1o RNA-binding proteins from rat brain.
Post-transcriptional regulation of mRNA metabolism is involved in processes as different as cell fate specification in development and cell response to a large variety of environmental cues. Regulation of all steps of RNA metabolism depends on RNA-binding proteins (RBPs). By using a T1 RNase-protection assay, we previously identified three H1 degrees RNA-binding factors (p40, p70 and p110), highly expressed in the rat brain. Here we report enrichment of these factors from brain extracts, obtained by affinity chromato-graphy of biotinylated H1 degrees RNA-protein complexes on streptavidin-conjugated paramagnetic particles. The purified proteins maintain RNA-binding ability and preference for histone messages.
Scaturrok
Maria
M
Dipartimento di Biologia Cellulare e dello Sviluppo Alberto Monroy, University of Palermo, Palermo, Italy.
Sala
Anna
A
Cutrona
Giuseppe
G
Raimondi
Lavinia
L
Cannino
Giuseppe
G
Fontana
Simona
S
Pucci-Minafra
Ida
I
Di Liegro
Italia
I
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002846:Chromatography, Affinity; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics / Q000302:isolation & purification*; D051381:Rats; D017207:Rats, Sprague-Dawley
D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D016601:RNA-Binding Proteins; D012313:RNA