Rat liver nuclear skeleton and small molecular weight RNA species.

Miller, Thomas E.; Huang, Ching-Hui; Pogo, A.O.

doi:10.1083/jcb.76.3.692

Cited by 97 publications

(22 citation statements)

References 30 publications

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“…Alternatively, piRNAs may act as a factor in the nuclear or cytoplasmic skeleton. Earlier results support this view: the attachment of small molecular-weight RNA species (smwRNAs) to the nuclear skeleton (Miller et al 1978), the localization of Doc RNA (retrotransposon) in the region of the cytoskeleton of the Drosophila oocyte (Zhao and Bownes 1998), and the localization of piRNA in the male mammalian meiotic nucleus (Marcon et al 2008). Cofactors may also influence piRNA functions; none has yet been identified in the ovary.…”

Section: Discussionmentioning

confidence: 99%

Profiling Sex-Specific piRNAs in Zebrafish

et al. 2010

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Piwi proteins and their partner small RNAs play an essential role in fertility, germ-line stem cell development, and the basic control and evolution of animal genomes. However, little knowledge exists regarding piRNA biogenesis. Utilizing microfluidic chip analysis, we present a quantitative profile of zebrafish piRNAs expressed differentially between testis and ovary. The sex-specific piRNAs are derived from separate loci of repeat elements in the genome. Ovarian piRNAs can be categorized into groups that reach up to 92 members, indicating a sex-specific arrangement of piRNA genes in the genome. Furthermore, precursor piRNAs preferentially form a hairpin structure at the 39end, which seem to favor the generation of mature sex-specific piRNAs. In addition, the mature piRNAs from both the testis and the ovary are 29-O -methylated at their 39 ends.

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Section: Discussionmentioning

confidence: 99%

Profiling Sex-Specific piRNAs in Zebrafish

et al. 2010

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“…Rat liver ribosomal RNA and cytoplasmic RNA were isolated by the phenol chloroform method (12). Rat liver nuclear RNA was isolated by the phenol-cresol method (12).…”

Section: Studies On the Specificity And Clinical Correlation Of Antirmentioning

confidence: 99%

“…Rat liver ribosomal RNA and cytoplasmic RNA were isolated by the phenol chloroform method (12). Rat liver nuclear RNA was isolated by the phenol-cresol method (12). Cytoplasmic RNA was fractionated into high and low molecular weight by centrifugation on 10 to 40% sucrose gradients (Figure 4).…”

Section: Studies On the Specificity And Clinical Correlation Of Antirmentioning

confidence: 99%

Studies on the Specificity and Clinical Correlation of Antiribosomal Antibodies in Systemic Lupus Erythematosus Sera

Koffler

Miller²,

Lahita

1979

Arthritis & Rheumatism

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The specificity of antibodies reactive with cytoplasmic ribosomes detected in systemic lupus erythematosus (SLE) sera was studied by a radioimmunoassay procedure with 3H labeled HeLa cell polysomes. The antibodies were directed primarily against RNA or a ribosomal RNA‐protein complex (rRNP). Anti‐RNA antibodies exhibited comparable reactivity with ribosomal RNA, nuclear RNA, structural RNA, and a slightly lower degree of reactivity with low molecular weight RNA. Anti‐rRNP antibodies may be detected by precipitation in agar gel and appear to require both the RNA and protein moieties of ribosomes for reactivity. SLE sera containing only anti‐rRNP antibodies are limited to patients with active disease. Sera from patients with both active and inactive SLE contain either anti‐RNA or a mixture of anti‐RNA and anti‐rRNP antibodies. The possible participation of anti‐ribosomal antibodies in immune complex formation is discussed.

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“…SnRNPs have been found in isolated nuclear matrices from rat liver (24), fibroblasts (37), chick oviduct cells (7) and bovine lymphocytes (26). In a previous paper (26), we demonstrated that bovine snRNPs could be dissociated both with a high salt buffer and a low salt buffer that contained ATP, calcium ion, EDTA and DTT and that their release was sensitive to magnesium ion.…”

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confidence: 80%

Small nuclear RNA-protein complex anchors on the actin filaments in bovine lymphocyte nuclear matrix.

Nakayasu

Ueda

1984

Cell Struct. Funct.

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ABSTRACT. When the nuclear matrix from bovine lymphocytes was digested by RNase-depleted trypsin, the bulk of the matrix proteins, except actin, were hydrolyzed. The digestion left rapidly sedimented spherical structures (trypsin-treated nuclear matrix), which mainly were composed of actin (Nakayasu, H. and K. Ueda. Exp. Cell Res. 143, 55-62, 1983). Almost all the small nuclear RNAs of the original nuclear matrix remained associated with these actin spheres after trypsin digestion.By sonication, the small nuclear RNPs (snRNPs) in both untreated and trypsin-treated nuclear matrices were solubilized in association with proteinous filaments of various size. The sedimentation pattern of these snRNP complexes was not changed by the digestion of the bulk of the proteins. The snRNP complex was adsorbed on rabbit muscle myosin-Sepharose then eluted by the addition of 5 mM ATP. We concluded that snRNPs are associated with actin filaments in the nuclear matrix of bovine lymphocytes.Nuclei of eucaryotic cells contain a fibrogranular complex, generally called the nuclear matrix (2,6,14). Except for its surface lamina, which consists mainly of lamin proteins (12,16,35), little has been reported on the meshwork of fibrous materials that traverse the nuclear interior. It is likely that this interior meshwork participates in such nuclear functions as DNA replication (9, 15, 31), RNA processing (18,21,23).Recently, we found that actin is a main component of the interior materials (27) in the bovine lymphocyte nuclear matrix. The existence of nuclear actin also has been reported in rat liver (9), Xenopus oocytes (8, 22), Physarum polycephalum (17), and dimethylsulfoxide-treated cells (11,34). The function of this nuclear actin, however, has yet to be determined.SnRNPs have been found in isolated nuclear matrices from rat liver (24), fibroblasts (37), chick oviduct cells (7) and bovine lymphocytes (26). In a previous paper (26), we demonstrated that bovine snRNPs could be dissociated both with a high salt buffer and a low salt buffer that contained ATP, calcium ion, EDTA and DTT and that their release was sensitive to magnesium ion. The conditions of release were closely related to the condition that causes the depolymerization of F-actin.

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Rat liver nuclear skeleton and small molecular weight RNA species.

Cited by 97 publications

References 30 publications

Profiling Sex-Specific piRNAs in Zebrafish

Profiling Sex-Specific piRNAs in Zebrafish

Studies on the Specificity and Clinical Correlation of Antiribosomal Antibodies in Systemic Lupus Erythematosus Sera

Small nuclear RNA-protein complex anchors on the actin filaments in bovine lymphocyte nuclear matrix.

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