Nucleic Acids Research, 2002, Vol. 30, No. 8 1725-1734
© 2002 Oxford University Press
Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins
1Department of Cell and Molecular Biology and 2Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Box 285, SE-171 77 Stockholm, Sweden and 3Institute of Biological Research and Biotechnology, The National Hellenic Research Foundation, Athens 11635, Greece
Pre-mRNP complexes were isolated from rat liver nuclei as 40S hnRNP particles, and actin-binding proteins were collected by DNase I affinity chromatography. The bound proteins were analyzed by 2D gel electrophoresis, and the following five hnRNP A/B-type proteins were identified by tandem mass spectrometry: DBP40/CBF-A (CArG binding factor A), a minor hnRNP A2 variant and three minor hnRNP A3 (mBx) variants. DBP40 was chosen for further analysis of the association of actin with the pre-mRNP complex. It was shown in vitro that purified actin binds to recombinant DBP40 suggesting that the interaction between actin and DBP40 is direct in the pre-mRNP particles. The association of actin with DBP40 was further explored in vivo. It was shown in a transfection study that DBP40 appears both in the nucleus and cytoplasm. Microinjection experiments revealed that DBP40 is exported from the nucleus to the cytoplasm. Finally, RNA–protein and protein–protein cross-linking experiments showed that DBP40 interacts with poly(A)+ RNA as well as actin, both in the nucleus and cytoplasm. We propose that actin associated with DBP40, and perhaps with additional hnRNP A/B-type proteins, is transferred from nucleus to cytoplasm bound to mRNA.
* To whom correspondence should be addressed. Tel: +46 8 7287370; Fax: +46 8 313529; Email: bertil.daneholt{at}cmb.ki.se
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