An ultrastructural characterization of in vitro-assembled hnRNP C protein-RNA complexes

Journal of Structural Biology
J E RechP F Flicker

Abstract

In mammalian cells approximately 700 nucleotide lengths of pre-mRNA are packaged during transcription by a unique group of abundant nuclear proteins to form a repeating array of regular ribonucleoprotein complexes termed 30-40S heterogeneous nuclear ribonucleoprotein particles (hnRNP particles). We have used electron microscopy to examine complexes that form when in vitro-transcribed RNA is bound by one of the purified native core-particle proteins which comprise the 40S monoparticle (the C protein tetramer). Negatively stained images of the C protein tetramer bound to particle-length RNA (700 nt) demonstrate that three tetramers bind each RNA molecule to form a stable closed triangular complex. The triangular complexes have an isosceles shape with a base of 18.0 nm and sides of 23.0 nm. When RNA molecules of 230 nt are used as substrates single tetramers bind to form complexes that appear as small rounded structures with an average diameter of 9.7 nm. Twice this length of RNA (456 nt) supports the assembly of mostly bilobed complexes that are 20.4 nm long and 11.8 nm wide. Images of the C protein-RNA complexes which assemble on 1400-nucleotide lengths of RNA (two particle lengths of RNA) clearly show complexes composed of two ...Continue Reading

Citations

Jul 3, 1998·Nucleic Acids Research·S R SoltaninassabW M LeStourgeon
Mar 30, 2011·Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology·David S Goodsell
Sep 13, 2014·Journal of the American Chemical Society·Zuzana CienikováChristophe Maris

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