Abstract
A major component of 30S heterogeneous nuclear ribonucleoprotein (hnRNP) particles from Artemia salina is HD40, a protein that has been characterized as a RNA helix-destabilizing protein [Marvil, D. K., Nowak, L. & Szer, W. (1980) J. Biol. Chem. 255, 6466-6472; Nowak, L., Marvil, D. K., Thomas, J. O., Boublik, M. & Szer, W. (1980) J. Biol. Chem. 255, 6473-6478]. HD40 binds to and disrupts the secondary structure of nuclear RNA fragments isolated from 30S hnRNP with a stoichiometry of one protein per 10-12 nucleotides. The addition of HD40 in excess of this ratio results in the formation of bead-like HD4-nuclear RNA complexes that are similar in properties and appearance to native 30S hnRNP particles. The heterogeneous nuclear RNA (hnRNA) in the HD40-hnRNA complexes is unstacked and unfolded to about the same extent as the RNA in the native 30S hnRNP particles. HD40 is strikingly similar in molecular weight (40,000) and amino acid composition (no cysteine, high glycine, presence of dimethylarginine, and blocked NH2 terminus) to eukaryotic hnRNP proteins isolated from many cell types. HD40 can be separated into three isoelectric species with basic pIs, which appears to be posttranslational modifications of a single polypeptide chain.
MeSH Terms
Animals
Artemia/enzymology
Cell Nucleus/enzymology
Circular Dichroism
DNA Helicases/isolation & purification
DNA-Binding Proteins
Microscopy, Electron
Nucleoproteins/isolation & purification
Protein Conformation
Ribonucleoproteins/isolation & purification
Viral Proteins
Chemicals
DNA-Binding Proteins
Nucleoproteins
Ribonucleoproteins
Viral Proteins
gp32 protein, Enterobacteria phage T4
helix-destabilizing proteins
DNA Helicases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Thomas J O
Raziuddin
Sobota A
Boublik M
Szer W
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