The PRP4 (RNA4) protein of Saccharomyces cerevisiae is associated with the 5′ portion of the U4 small nuclear RNA

Yan Xu, Sara Petersen-Bjørn, James D. Friesen

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

We have combined oligonucleotide-directed RNase H degradation and immunoprecipitation in a study of the association of the Saccharomyces cerevisiae PRP4 protein with the U4-U6 complex. We have found that three oligonucleotides were able to direct nearly to completion the RNase H-specific cleavage of the target RNA molecules as they exist in splicing extracts. Immunoprecipitation of the degradation products with PRP4 antibody showed that the 5′ portion of U4 small nuclear RNA (snRNA) and the 3′ portion of U6 snRNA coimmunoprecipitated with the PRP4 protein. Micrococcal nuclease protection experiments confirmed further that the 5′ portion and 3′ end of U4 snRNA were very resistant to nuclease digestion, whereas the 3′ portion of U6 snRNA was protected to only a very small extent. We conclude that the PRP4 protein of S. cerevisiae is associated primarily with the 5′ portion of U4 snRNA in the U4-U6 small nuclear ribonucleoprotein (snRNP).

Original languageEnglish
Pages (from-to)1217-1225
Number of pages9
JournalMolecular and Cellular Biology
Volume10
Issue number3
StatePublished - 1990
Externally publishedYes

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Saccharomyces cerevisiae Proteins
Ribonuclease H
Immunoprecipitation
Oligonucleotides
U4-U6 Small Nuclear Ribonucleoproteins
RNA Cleavage
Micrococcal Nuclease
Digestion
Antibodies
U4 small nuclear RNA
Proteins
U6 small nuclear RNA

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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The PRP4 (RNA4) protein of Saccharomyces cerevisiae is associated with the 5′ portion of the U4 small nuclear RNA. / Xu, Yan; Petersen-Bjørn, Sara; Friesen, James D.

In: Molecular and Cellular Biology, Vol. 10, No. 3, 1990, p. 1217-1225.

Research output: Contribution to journalArticle

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abstract = "We have combined oligonucleotide-directed RNase H degradation and immunoprecipitation in a study of the association of the Saccharomyces cerevisiae PRP4 protein with the U4-U6 complex. We have found that three oligonucleotides were able to direct nearly to completion the RNase H-specific cleavage of the target RNA molecules as they exist in splicing extracts. Immunoprecipitation of the degradation products with PRP4 antibody showed that the 5′ portion of U4 small nuclear RNA (snRNA) and the 3′ portion of U6 snRNA coimmunoprecipitated with the PRP4 protein. Micrococcal nuclease protection experiments confirmed further that the 5′ portion and 3′ end of U4 snRNA were very resistant to nuclease digestion, whereas the 3′ portion of U6 snRNA was protected to only a very small extent. We conclude that the PRP4 protein of S. cerevisiae is associated primarily with the 5′ portion of U4 snRNA in the U4-U6 small nuclear ribonucleoprotein (snRNP).",
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N2 - We have combined oligonucleotide-directed RNase H degradation and immunoprecipitation in a study of the association of the Saccharomyces cerevisiae PRP4 protein with the U4-U6 complex. We have found that three oligonucleotides were able to direct nearly to completion the RNase H-specific cleavage of the target RNA molecules as they exist in splicing extracts. Immunoprecipitation of the degradation products with PRP4 antibody showed that the 5′ portion of U4 small nuclear RNA (snRNA) and the 3′ portion of U6 snRNA coimmunoprecipitated with the PRP4 protein. Micrococcal nuclease protection experiments confirmed further that the 5′ portion and 3′ end of U4 snRNA were very resistant to nuclease digestion, whereas the 3′ portion of U6 snRNA was protected to only a very small extent. We conclude that the PRP4 protein of S. cerevisiae is associated primarily with the 5′ portion of U4 snRNA in the U4-U6 small nuclear ribonucleoprotein (snRNP).

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