Fractionation of HeLa cell nuclear extracts reveals minor small nuclear ribonucleoprotein particles.
AUTOR(ES)
Krämer, A
RESUMO
Upon chromatographic fractionation of HeLa cell nuclear extracts, small RNAs of 145 and 66/65 nucleotides, respectively, were detected that are distinct from the abundant small RNAs present in the extract. These RNAs are precipitated by antibodies directed against the trimethylguanosine cap structure, characteristic for small nuclear RNAs (snRNAs) of the U type. The RNAs of 145 and 66/65 nucleotides appear to be associated with at least one of the proteins common to the major small nuclear ribonucleoprotein particles U1 to U6, since they are specifically bound by anti-Sm antibodies. These criteria characterize the RNAs that are 145 and 66/65 nucleotides in length as U-type snRNAs. Upon gel filtration, the RNAs are found within particles of molecular weights approximately equal to 150,000 and 115,000, respectively. The RNA of 145 nucleotides represents a different minor snRNA, designated U11, whereas the RNA of 66/65 nucleotides may correspond to either mammalian U7 or U10 RNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=299552Documentos Relacionados
- Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles.
- Polypeptide components of Drosophila small nuclear ribonucleoprotein particles.
- Affinity purification of transcription factor IIA from HeLa cell nuclear extracts.
- Purification of histone messenger ribonucleoprotein particles from HeLa cell S-phase polysomes. Characterization of associated proteins
- Higher order nuclear organization: three-dimensional distribution of small nuclear ribonucleoprotein particles.
