Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts

Biochemistry
S B AmruteM J Modak

Abstract

A single-strand nucleic acid binding protein (C/F) that has an apparent molecular weight of 12,000 on SDS-polyacrylamide gel electrophoresis and that was originally thought to be the 12-kDa alpha-subunit of the AB form of terminal deoxynucleotidyl transferase (TdT) from calf thymus has been purified and identified as a fragment of the type C1/C2 hnRNP proteins. On the basis of NH2-terminal sequencing and mass spectrometric analysis, C/F contains approximately 94 residues and spans from residue 9 to approximately residue 102 in the type C1/C2 hnRNP proteins. C/F is presumably produced in vitro via limited proteolysis of the type C1/C2 hnRNP proteins following cell disruption. Since C/F corresponds almost exactly to the approximately 90-residue conserved ribonucleoprotein binding domain (RBD) that is shared by many eukaryotic RNA binding proteins, it provided an opportunity to better characterize the domain structure of the type C1/C2 hnRNP proteins and to compare the nucleic acid binding properties of the type C1/C2 and A1 [see Shamoo et al. (1994) Biochemistry, preceding paper in this issue] RNA binding domains. Like the type A1 RBD, the type C1/C2 RBD has an apparent occluded site size of 6-7 nucleotides. The type C1/C2 RBD bi...Continue Reading

Citations

Dec 22, 1999·Biochemical and Biophysical Research Communications·S Y YingS Lin
Mar 11, 1995·Nucleic Acids Research·Y ShamooK R Williams
Jul 3, 1998·Nucleic Acids Research·S R SoltaninassabW M LeStourgeon
Dec 7, 2007·The EMBO Journal·Gregg V CrichlowDemetrios Braddock

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