Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae - PubMed (original) (raw)

Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae

S M Wilson et al. J Cell Biol. 1994 Dec.

Abstract

To study the functions of heterogeneous nuclear ribonucleoproteins (hnRNPs), we have characterized nuclear polyadenylated RNA-binding (Nab) proteins from Saccharomyces cerevisiae. Nab1p, Nab2p, and Nab3p were isolated by a method which uses UV light to cross-link proteins directly bound to poly(A)+ RNA in vivo. We have previously characterized Nab2p, and demonstrated that it is structurally related to human hnRNPs. Here we report that Nab1p is identical to the Np13p/Nop3p protein recently implicated in both nucleocytoplasmic protein shuttling and pre-rRNA processing, and characterize a new nuclear polyadenylated RNA-binding protein, Nab3p. The intranuclear distributions of the Nab proteins were analyzed by three-dimensional immunofluorescence optical microscopy. All three Nab proteins are predominantly localized within the nucleoplasm in a pattern similar to the distribution of hnRNPs in human cells. The NAB3 gene is essential for cell viability and encodes an acidic ribonucleoprotein. Loss of Nab3p by growth of a GAL::nab3 mutant strain in glucose results in a decrease in the amount of mature ACT1, CYH2, and TPI1 mRNAs, a concomitant accumulation of unspliced ACT1 pre-mRNA, and an increase in the ratio of unspliced CYH2 pre-mRNA to mRNA. These results suggest that the Nab proteins may be required for packaging pre-mRNAs into ribonucleoprotein structures amenable to efficient nuclear RNA processing.

PubMed Disclaimer

Cited by

Role and molecular mechanism of heterogeneous nuclear ribonucleoprotein K in tumor development and progression.
Lu J, Gao FH. Lu J, et al. Biomed Rep. 2016 Jun;4(6):657-663. doi: 10.3892/br.2016.642. Epub 2016 Mar 29. Biomed Rep. 2016. PMID: 27284403 Free PMC article.
The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.
Anderson J, Phan L, Cuesta R, Carlson BA, Pak M, Asano K, Björk GR, Tamame M, Hinnebusch AG. Anderson J, et al. Genes Dev. 1998 Dec 1;12(23):3650-62. doi: 10.1101/gad.12.23.3650. Genes Dev. 1998. PMID: 9851972 Free PMC article.
Control of cleavage site selection during mRNA 3' end formation by a yeast hnRNP.
Minvielle-Sebastia L, Beyer K, Krecic AM, Hector RE, Swanson MS, Keller W. Minvielle-Sebastia L, et al. EMBO J. 1998 Dec 15;17(24):7454-68. doi: 10.1093/emboj/17.24.7454. EMBO J. 1998. PMID: 9857200 Free PMC article.
Myotonic dystrophy: molecular windows on a complex etiology.
Korade-Mirnics Z, Babitzke P, Hoffman E. Korade-Mirnics Z, et al. Nucleic Acids Res. 1998 Mar 15;26(6):1363-8. doi: 10.1093/nar/26.6.1363. Nucleic Acids Res. 1998. PMID: 9490778 Free PMC article. Review.
A genetic screen for terminator function in yeast identifies a role for a new functional domain in termination factor Nab3.
Loya TJ, O'Rourke TW, Reines D. Loya TJ, et al. Nucleic Acids Res. 2012 Aug;40(15):7476-91. doi: 10.1093/nar/gks377. Epub 2012 May 7. Nucleic Acids Res. 2012. PMID: 22564898 Free PMC article.

References

1. Exp Cell Res. 1973 Aug;80(2):313-21 - PubMed
1. Trends Genet. 1991 Mar;7(3):79-85 - PubMed
1. Proc Natl Acad Sci U S A. 1980 Jul;77(7):3912-6 - PubMed
1. J Mol Appl Genet. 1982;1(5):419-34 - PubMed
1. Nucleic Acids Res. 1983 May 25;11(10):3123-35 - PubMed

Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae - PubMed (original) (raw)