Note. The nucleotide sequence of MII is available under EMBL accession number L23999.
Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 221, Issue 2, pages 749–757, April 1994
How to Cite
FACKELMAYER, F. O., DAHM, K., RENZ, A., RAMSPERGER, U. and RICHTER, A. (1994), Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro. European Journal of Biochemistry, 221: 749–757. doi: 10.1111/j.1432-1033.1994.tb18788.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received October 10, 1993/February 10, 1994) – EJB 93 1574/2
We show that SAF-A, a nuclear protein which specifically binds vertebrate scaffold-attachmentregion (SAR) elements with high affinity is identical with hnRNP-U, assumed to be involved in packaging of hnRNA in ribonucleoprotein particles. Ultraviolet cross-linking experiments show that the protein, referred to as hnRNP-U/SAF-A, is bound to chromosomal DNA in vivo. In vitro, the isolated protein binds to double-stranded and single-stranded DNA and forms higher ordered nucleic-acid–protein complexes. Filter-binding experiments performed with different types of natural and synthetic nucleic acids as substrates show that the protein binds DNA and RNA with different affinities and most likely at different binding sites. We conclude that hnRNP-U/SAF-A thus may have functions in the organisation of chromosomal DNA in addition to its suggested role in hnRNA metabolism.