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3 edition of Structure and metabolism of nuclear polyadenylate-protein complexes from mouse ascites cells found in the catalog.

Structure and metabolism of nuclear polyadenylate-protein complexes from mouse ascites cells

Thomas Joseph Quinlan

Structure and metabolism of nuclear polyadenylate-protein complexes from mouse ascites cells

by Thomas Joseph Quinlan

  • 308 Want to read
  • 10 Currently reading

Published .
Written in English


Classifications
LC ClassificationsMicrofilm 45664
The Physical Object
FormatMicroform
Paginationix, 114 l.
Number of Pages114
ID Numbers
Open LibraryOL1367784M
LC Control Number92895080

In eukaryotes, thousands of genes have to be organized and expressed in the cell nucleus. Conformational and kinetic instability of nuclear structure and components appear to enable cells to use the encoded information selectively. The ubiquitin-proteasome system is active in distinct nuclear domains and plays a major role controlling the initial steps of gene expression, DNA repair and. The glycolytic rate in single living ascites cells can be estimated at room temperature and 37 °C in a Chance-Legallais microfluorimeter from the half-life of the transient pyridine nucleotide.

  In fact, we have previously demonstrated that it is possible to isolate from the nucleus a complex that is associated to inner nuclear membrane and constituted by proteins, PC-SM-CHO, enzymes for lipid metabolism and newly synthesized RNA (Rossi et al., a,b). In the present work, we obtained through biochemical isolation of microdomains, a. The Periodic Structure of Nuclear and Cytoplasmic Crystals of Dog Liver Cells Observations of Rabbit Leucocytic Pyrogen Ultrastructure of Yolk Platelets in the Amphibian Egg Electron Microscopic Ultrastructure of the Elastic Fiber Evidence for a Complex Internal Structure in Certain Collagen Fibrils Ultrastructure of Collagen Fibrils.

The nucleus is the largest organelle in animal cells. In mammalian cells, the average diameter of the nucleus is approximately 6 micrometres (µm), which occupies about 10% of the total cell volume. The contents of the nucleus are held in the nucleoplasm similar to the cytoplasm in the rest of the cell. The fluid component of this is termed the nucleosol, similar to the cytosol in the cytoplasm. Martin TE, McCarthy BJ. Synthesis and turnover of RNA in the S nuclear ribonucleoprotein complexes of mouse ascites cells. Biochim Biophys Acta. Aug 25; (2)– Pederson T. Proteins associated with heterogeneous nuclear RNA in eukaryotic cells. J .


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Structure and metabolism of nuclear polyadenylate-protein complexes from mouse ascites cells by Thomas Joseph Quinlan Download PDF EPUB FB2

Abstract. Nuclear poly(A)-containing RNA of mouse ascites cells can be extracted in the form of S ribonucleoprotein complexes under conditions in which the bulk of the heterogeneous nuclear RNA is released as 30S by:   Properties of a nuclear polyadenylate-protein complex from mouse ascites cells.

Quinlan TJ, Kinniburgh AJ, Martin TE. Ribonucleoprotein (RNP) subcomplexes containing at least 60% of the total nuclear poly(A) were isolated from mouse ascites cells; these 15 S ribonucleoprotein particles were most probably derived from larger hnRNA containing Cited by: Martin, T.E., McCarthy, B.J.: Synthesis and turnover of RNA in the S nuclear ribonucleoprotein complexes of mouse ascites cells.

Biochim biophys. Acta (Amst.) Cited by: Properties of a nuclear polyadenylate-protein complex from mouse ascites cells. T J Quinlan, A J Kinniburgh, Expression of genes for metabolism of cyclic adenosine 3':5'-monophosphate in somatic cells. beta-Adrenergic and PGE1 receptors in parental and hybrid cells.

The poly(A) sequences at the 3′ end of mRNA and nuclear RNA molecules of mouse sarcoma and Chinese hamster cells are subject to an elongation process distinct from de novo synthesis. This process continues in cells treated with a high level of actinomycin D to block transcription.

This results in the labeling of the steady-state poly(A) population in the cytoplasm and of unusually long poly Cited by: ABSTRACT Nuclear poly(A)-containingRNAofmouse ascites cells can be extracted in the formofS ribo-nucleoprotein complexes under conditions in whichthe bulkoftheheterogeneous nuclearRNAis released as 30S complexes.

The poly(A)-containing fraction of nuclear extracts has been resolved into two distinct components. Request PDF | OnPeter C. Heinrich and others published Structure and function of nuclear ribonucleoprotein complexes | Find, read and cite all the research you need on ResearchGate.

Cell Biology International Reports, Vol. 3, No. 4, POLYADENYLATE-PROTEIN COMPLEXES IN RESTING AND GROWING 3T3 CELLS Everett Bandrnan* and Ajit Kumar** Cell Biology Unit, Shriners Burns Institute, Boston, Massachusetts 51 Blossom Street, ABSTRACT The properties of the ribonuclease resistant cyto- plasmic ribonucleoprotein particles were studied in.

Since it has been reported from this laboratory that the nucleoli of mouse ascites tumour cells are incapable of synthesizing proteins via a typical ribosomal system, the possibility of transfer of newly synthesized protein molecules to the nucleoli from other cellular components was tested.

Pulse-chase experiments of amino acids were carried out on ascites tumour cells cultivated. Total low molecular weight nuclear RNAs of mouse ascites cells have been labeled in vitro and used as probes to search for complementary sequences contained in nuclear or cytoplasmic RNA.

Similar results are obtained with yeast and mouse fibroblasts, indicating a high degree of conservation of both nuclear and cytoplasmic polyadenylate-binding proteins.

The activity from rat liver nuclei has been purified fold on the basis of specific binding to polyadenylate and shows two main bands in sodium dodecyl sulfate gels at 53 and.

Since it has been reported from this laboratory that the nucleoli of mouse ascites tumour cells are incapable of synthesizing proteins via a typical r. A protein complex or multiprotein complex is a group of two or more associated polypeptide ent polypeptide chains may have different functions.

This is distinct from a multienzyme complex, in which multiple catalytic domains are found in a single polypeptide chain. Protein complexes are a form of quaternary structure. Proteins in a protein complex are linked by non-covalent. From Adherent Cells. Grow cells to % confluency. Remove the growth medium from the cells.

Rinse the cells twice with PBS, being careful not to dislodge any cells. Discard the PBS. Scrape the cells using fresh PBS and collect into an appropriate conical centrifuge tube.

Centrifuge for 5 minutes at x g. Decant and discard the supernatant. Topics include carbohydrate metabolism of ascites tumor cells, comparative biochemistry of glycolysis, DNA and the genetic concept of cancer, and constancy of free amino acid patterns of tissues.

The selection is a valuable source of data for biochemists and researchers interested in amino acids, proteins, and cancer biochemistry. The oculopharyngeal muscular dystrophy (OPMD) protein PABN1 regulates selection of alternative mRNA polyadenylation sites by binding to and suppressing the use of proximal sequences.

Consequently, triplet-repeat expansion of the PABN1 gene in human OPMD results in widespread shortening of target mRNAs, contributing to pathogenesis of the disease.

Biophysical Perspective Protein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine Tijana Jovanovic-Talisman1,* and Anton Zilman2,3,* 1Department of Molecular Medicine, Beckman Research Institute of the City of Hope Comprehensive Cancer Center, Duarte, California; 2Department of Physics and 3Institute for Biomaterials and Biomedical Engineering.

The three-dimensional structure of the pore complex has been determined by electron microscopic analysis to a resolution of w90 A (Unwin and Milligan, ). The pore complex is a symmetrical structure consisting of two coaxial annuli, one of which faces the cytosol and the other the nucleoplasm. IPO7 is functioning in the nuclear import of proteins and is known to be located at both the nucleoplasmic and cytoplasmic side of the nuclear pore complex (detected in A cells).

RRAGC is shuttling between the nucleus and the cytoplasm. It plays a crucial role in the initiation of the TOR signaling cascade where it is required for the amino. Analysis of polyadenylate. protein complex of polysomal messenger RNA from mouse L cells.

Bernd A, Zahn RK, Maidhof A, Müller WE. The organization of polysomal poly(A)-ribonucleoprotein complex [poly(A)-RNP] was studied. The poly(A)-associated proteins were liberated directly from the poly(A)-RNP complex.

1. The conditions are described in which the microfluorimetric-microelectrophoretic technique can be used for a comparative study of fluorescence changes due to reduced pyridine nucleotides in the cytoplasm and nucleus of irradiated and non-irradiated Chang and EL2 cells, treated with a variety of glycolytic substrates.

So far there is considerable simultaneity in the nuclear and cytoplasmic.SUN2 is known to be part of the LINC protein complexes that enables connection of the cytoskeleton to the nuclear membrane (detected in A cells). 1% ( proteins) of all human proteins have been experimentally detected in the nuclear membrane by the Human Protein Atlas.Kenta Nakai, Kenichiro Imai, in Encyclopedia of Bioinformatics and Computational Biology, Prediction of nuclear localization signals and nuclear export signals.

Nuclear proteins are carried into and out of the nuclei through the nuclear pore complex by nucleocytoplasmic transport receptors, that is, the importin (karyopherin)-β family. The human genome encodes 20 importin-β family.