Characterization of an RNP complex that assembles on the Rous sarcoma virus negative regulator of splicing element. Nucleic Acids Res 1996 Dec 15;24(24):4962-8
Date
12/15/1996Pubmed ID
9016667Pubmed Central ID
PMC146344DOI
10.1093/nar/24.24.4962Scopus ID
2-s2.0-0030459517 (requires institutional sign-in at Scopus site) 7 CitationsAbstract
We have characterized an RNP complex that assembles in nuclear extracts on the negative regulator of splicing (NRS) element from Rous sarcoma virus. While no complex was detected by native gel electrophoresis under conditions that supported spliceosome assembly, gel filtration revealed a specific ATP-independent complex that rapidly assembled on NRS RNA. No complexes were formed on non-specific RNA. Unlike the non-specific H complex, factors required for NRS complex assembly are limiting in nuclear extract. The NRS complex was not detected in reactions containing ATP and pre-formed complexes were dissociated in the presence of ATP. In addition, the assembly process was sensitive to high salt but NRS complexes were salt stable once formed. Assembly of the NRS complex appears functionally significant since mutated NRS RNAs that fail to inhibit splicing in vivo are defective for NRS complex assembly in nuclear extract. The probable relationship of the NRS complex to spliceosomal complexes is discussed.
Author List
Cook CR, McNally MTAuthor
Mark T. McNally PhD Associate Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adenosine TriphosphateAvian Sarcoma Viruses
Chromatography, Gel
Kinetics
Plasmids
RNA Splicing
Ribonucleoproteins
Spliceosomes