Different complexes are formed on the 3′ end of histone mRNA with nuclear and polyribosomal proteins

Niranjan Pandey, Jian Hua Sun, William F. Marzluff

Research output: Contribution to journalArticle

Abstract

Specific protein-RNA complexes are formed by incubating a synthetic histone mRNA 3′ end (a 30 nucleotide stem-loop structure) RNA with extracts of either nuclei or polyribosomes. The complex formed between the stem-loop and nuclear proteins has a lower electrophoretic mobility than the complex formed between the stem-loop and polyribosomal proteins. Binding of the synthetic 3′ end by both polyribosomal and nuclear proteins is abolished when two of the conserved uridine residues in the loop are replaced with adenosines. UV crosslinking of the protein complexes to the synthetic RNA resulted in transferring radiolabel to similar sized proteins, 50 kD, in both the nuclear and polyribosomal extracts.

Original languageEnglish (US)
Pages (from-to)5653-5659
Number of pages7
JournalNucleic Acids Research
Volume19
Issue number20
StatePublished - Oct 25 1991
Externally publishedYes

Fingerprint

Nuclear Proteins
Messenger RNA
Histones
RNA
Proteins
Protein
Electrophoretic mobility
Polyribosomes
Uridine
Nucleotides
Crosslinking
Adenosine
Nucleus

ASJC Scopus subject areas

  • Genetics
  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Health, Toxicology and Mutagenesis
  • Toxicology
  • Genetics(clinical)

Cite this

Different complexes are formed on the 3′ end of histone mRNA with nuclear and polyribosomal proteins. / Pandey, Niranjan; Sun, Jian Hua; Marzluff, William F.

In: Nucleic Acids Research, Vol. 19, No. 20, 25.10.1991, p. 5653-5659.

Research output: Contribution to journalArticle

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