Macromolecular domains containing nuclear protein p107 and U-snRNP protein p28: further evidence for an in situ nuclear matrix

Smith, H. C., Ochs, R. L., Fernandez, E. A., Spector, D. L. (1986) Macromolecular domains containing nuclear protein p107 and U-snRNP protein p28: further evidence for an in situ nuclear matrix. Molecular and Cellular Biology, 70 (2). pp. 151-168. ISSN 0270-7306

URL: http://www.ncbi.nlm.nih.gov/pubmed/2941679
DOI: 10.1007/BF00229430

Abstract

Polyclonal antibodies have been produced which react with a nuclear protein having a molecular weight of 107kD and a pI of 8.7-8.8 (designated p107). This protein is shown to be a component of the residual ribonucleoprotein (RNP) network of the nuclear matrix. P107 localized exclusively to the nuclear interior but not within nucleolar or chromatin domains. We have taken advantage of this unique probe to examine whether the RNP network of the isolated nuclear matrix has a physical counterpart in situ. We show that RNA, p107, divalent cations and the 28 kD Sm antigen of U-snRNPs are components of in situ macromolecular assemblies. While the morphology and intranuclear distribution of these assemblies are insensitive to the removal of chromatin, they are markedly altered by degradation of RNA. Digestion in situ of RNA in the presence of EDTA followed by extraction with high ionic strength buffers solubilized the components of these assemblies. Electron microscopic and immunobiochemical data are presented which support the concept that the residual RNP network of the nuclear matrix is an isolate of a pre-existing structure, and that perturbations in this internal network can be created by RNA degradation, depletion of essential metal ions and proteolysis.

Item Type: Paper
Uncontrolled Keywords: Animals Cell Nucleus Edetic Acid Fluorescent Antibody Technique Immunosorbent Techniques Isoelectric Point Male Microscopy, Electron Molecular Weight Rats Ribonucleoproteins Ribonucleoproteins, Small Nuclear Solubility Transcription, Genetic
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > matrix protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > proteolysis
CSHL Authors:
Communities: CSHL labs > Spector lab
Depositing User: Matt Covey
Date Deposited: 10 Dec 2012 19:43
Last Modified: 29 Jan 2015 20:52
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26314

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