Work

Classification and Purification of Proteins of Heterogeneous Nuclear Ribonucleoprotein Particles by RNA-Binding Specificities

Year: 1988

Type: article

Abstract: Several proteins of heterogeneous nuclear ribonucleoprotein (hnRNP) particles display very high binding affinities for different ribonucleotide homopolymers. The specificity of some of these proteins at high salt concentrations and in the presence of heparin allows for their rapid one-step purification from HeLa nucleoplasm. We show that the hnRNP C proteins are poly(U)-binding proteins and compare their specificity to that of the previously described cytoplasmic poly(A)-binding protein. These findings provide a useful tool for the classification and purification of hnRNP proteins from various tissues and organisms and indicate that different hnRNP proteins have different RNA-binding specificities.

Source: Molecular and Cellular Biology

DOI: 10.1128/mcb.8.5.2237-2241.1988

Authors: M S Swanson, G Dreyfuss

Institution: Northwestern University

Language: English

Topic: RNA Research and Splicing

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: American Heart Association, National Institutes of Health, National Institute of General Medical Sciences

Awards: STRUCTURE AND FUNCTION OF NUCLEAR RNP PARTICLES, RIBONUCLEOPROTEINS, MRNA AND CYTOSKELETAL STRUCTURES