Cytoplasmic assembly of snRNP particles from stored proteins and newly transcribed snRNA's in L929 mouse fibroblasts

Sauterer, Roger; Feeney, Robert J.; Zieve, Gary W.

doi:10.1016/0014-4827(88)90336-9

Cited by 67 publications

(46 citation statements)

References 37 publications

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“…The snRNP proteins in the gradient in Fig. 6 show a similar distribution of RNA-free intermediates, as described previously (17). The B proteins were found in a heterodispersed set of structures sedimenting at from 2S to 20S; the D, E, F, and G proteins were found at 6S.…”

Section: Resultssupporting

confidence: 80%

“…6, lanes 10 and 11). The (17). Gradient fractions were immunoprecipitated with the Y12 anti-Sm MCA and resolved on 13% gels containing 1.5 M urea. Lanes are marked according to the gradient fraction, beginning at the top.…”

Section: Resultsmentioning

confidence: 99%

“…Gradient fractions were immunoprecipitated with the Y12 anti-Sm MCA and resolved on 13% gels containing 1.5 M urea. Lanes are marked according to the gradient fraction, beginning at the top. S values were determined from the mobilities of standard proteins in a parallel gradient as described previously (17).…”

Section: Resultsmentioning

confidence: 99%

“…In standard SDS-polyacrylamide gels, the D' and D snRNP core proteins comigrate at approximately 16 kilodaltons. The [4832][4833][4834][4835][4836]1988).…”

mentioning

confidence: 99%

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Identification and characterization of the small nuclear ribonucleoprotein particle D' core protein.

1990

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The addition of urea to sodium dodecyl sulfate (SDS)-polyacrylamide gels has allowed the identification and characterization of the small nuclear ribonucleoprotein particle (snRNP) D Small nuclear ribonucleoprotein particles (snRNPs) contain a unique small nuclear RNA (snRNA) with several snRNP-specific proteins in addition to a common core of proteins shared by almost all the snRNPs. The major snRNPs in the nucleoplasm share a group of core proteins that includes the previously identified B, D, E, F, and G proteins (for reviews, see references 3 and 20a). There are tissue-and species-specific differences in the B protein, including an alternatively spliced B' protein present in most primate but not murine tissues (1Sa, 18). The newly synthesized snRNP core proteins are stored in large snRNA-free pools in the cytoplasm and are available for assembly with newly transcribed snRNAs that appear transiently in the cytoplasm. The snRNP core proteins move into the nucleus after being assembled into snRNPs. The snRNP B protein is the first core protein to accumulate in the nucleus, suggest-

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Section: Resultssupporting

confidence: 80%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…In standard SDS-polyacrylamide gels, the D' and D snRNP core proteins comigrate at approximately 16 kilodaltons. The [4832][4833][4834][4835][4836]1988).…”

mentioning

confidence: 99%

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Identification and characterization of the small nuclear ribonucleoprotein particle D' core protein.

1990

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“…This is in agreement with previous studies in mice, which show that a reduction in the embryo-specific U1b snRNA level is only detectable in 11 to 19-d-old embryos (Cheng et al 1997). This might reflect that vU1 snRNAs are as stable as the U1 snRNA, which has an estimated half-life of 4-5 d (Sauterer et al 1988). This data indicates that regulation of vU1 snRNA gene activity occurs early in the differentiation process, possibly allowing time for steady-state levels of vU1 snRNAs to reduce before the hEBs differentiate into different cell types.…”

Section: Some Vu1 Snrna Genes Are Differentially Expressedmentioning

confidence: 89%

Differentially expressed, variant U1 snRNAs regulate gene expression in human cells

et al. 2012

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Human U1 small nuclear (sn)RNA, required for splicing of pre-mRNA, is encoded by genes on chromosome 1 (1p36). Imperfect copies of these U1 snRNA genes, also located on chromosome 1 (1q12-21), were thought to be pseudogenes. However, many of these “variant” (v)U1 snRNA genes produce fully processed transcripts. Using antisense oligonucleotides to block the activity of a specific vU1 snRNA in HeLa cells, we have identified global transcriptome changes following interrogation of the Affymetrix Human Exon ST 1.0 array. Our results indicate that this vU1 snRNA regulates expression of a subset of target genes at the level of pre-mRNA processing. This is the first indication that variant U1 snRNAs have a biological function in vivo. Furthermore, some vU1 snRNAs are packaged into unique ribonucleoproteins (RNPs), and many vU1 snRNA genes are differentially expressed in human embryonic stem cells (hESCs) and HeLa cells, suggesting developmental control of RNA processing through expression of different sets of vU1 snRNPs.

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Assembly and intracellular transport of snRNP particles

Andersen¹,

Zieva²

1991

BioEssays

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The assembly of the major small nuclear ribonucleoprotein (snRNP) particles begins in the cytoplasm where large pools of common core proteins are preassembled in several RNA-free intermediate particles. Newly synthesized snRNAs transiently enter the cytoplasm and complex with core particles to form pre-snRNP particles. Subsequently, the cap structure at the 5' end of the snRNA is hypermethylated. The resulting trimethylguanosine (TMG) cap is an integral part of the nuclear localization signal for snRNP particles and the pre-snRNP particles are rapidly transported into the nucleus. SnRNP particles mature when snRNA-specific proteins complex with the particles, in some cases, just before or during nuclear transport, but in most instances after the particles are in the nucleus. In addition, U6 snRNA hybridizes with U4 snRNA to form a U4/U6 snRNP in the nucleus. The transport signals are retained on the snRNP particles and proteins since existing particles and proteins enter the reformed nucleus after mitosis.

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Cytoplasmic assembly of snRNP particles from stored proteins and newly transcribed snRNA's in L929 mouse fibroblasts

Cited by 67 publications

References 37 publications

Identification and characterization of the small nuclear ribonucleoprotein particle D' core protein.

Identification and characterization of the small nuclear ribonucleoprotein particle D' core protein.

Differentially expressed, variant U1 snRNAs regulate gene expression in human cells

Assembly and intracellular transport of snRNP particles

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