Artigo Acesso aberto Revisado por pares

An abundant U6 snRNP found in germ cells and embryos of Xenopus laevis.

1989; Springer Nature; Volume: 8; Issue: 13 Linguagem: Inglês

10.1002/j.1460-2075.1989.tb08603.x

ISSN

1460-2075

Autores

Jörg Hamm, Iain W. Mattaj,

Tópico(s)

RNA and protein synthesis mechanisms

Resumo

Research Article20 December 1989free access An abundant U6 snRNP found in germ cells and embryos of Xenopus laevis. J. Hamm J. Hamm EMBL Heidelberg, FRG. Search for more papers by this author I.W. Mattaj I.W. Mattaj EMBL Heidelberg, FRG. Search for more papers by this author J. Hamm J. Hamm EMBL Heidelberg, FRG. Search for more papers by this author I.W. Mattaj I.W. Mattaj EMBL Heidelberg, FRG. Search for more papers by this author Author Information J. Hamm1 and I.W. Mattaj1 1EMBL Heidelberg, FRG. The EMBO Journal (1989)8:4179-4187https://doi.org/10.1002/j.1460-2075.1989.tb08603.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The particle state of U snRNPs was analyzed in oocytes, eggs, embryos and testes from Xenopus laevis. In each case both the relative abundance and the composition of some U snRNPs were found to differ from that of somatic cells. U2 and U6 snRNPs were the most prominent U snRNPs in germ cells and early embryos. In particular, the concentration of U6 snRNA was 10-20 times higher than that of U4 snRNA. Most of the U6 snRNA was not associated with U4 snRNA and migrated on sucrose gradients as a U6 snRNP. The structure of this novel U snRNP was analyzed. A single protein of 50 kd was copurified with U6 snRNPs by a combination of gradient fractionation, immunodepletion with anti-Sm antibodies and immunoprecipitation with anti-6-methyl adenosine antibodies. Although the U6 snRNP did not contain Sm proteins it migrated into the nucleus when U6 snRNA was injected into the cytoplasm of oocytes. Two U6 snRNA elements have been identified. The first is essential for nuclear migration in oocytes, but not for the formation of U4/6 snRNPs in vitro and might be the binding site of a U6-specific protein. The second element was required for interaction with U4 snRNPs but not for nuclear targeting. Previous ArticleNext Article Volume 8Issue 131 December 1989In this issue RelatedDetailsLoading ...

Referência(s)
Altmetric
PlumX