Subcellular compartmentalization of mRNAs

Bagchi, Tamishraha (1986) Subcellular compartmentalization of mRNAs. Masters thesis, Memorial University of Newfoundland.

[img] [English] PDF (Migrated (PDF/A Conversion) from original format: (application/pdf)) - Accepted Version
Available under License - The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission.

Download (12Mb)
  • [img] [English] PDF - Accepted Version
    Available under License - The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission.
    (Original Version)

Abstract

The importance of the cytoskeleton in protein synthesis was studied in differentiating L6 rat myoblasts. Soluble and cytoskeletal fractions obtained after gentle, non-ionic detergent lysis of myoblasts and myotubes were analysed for the presence of ribosomes and mRNPs. The role of the cytoskeleton in compartmentalization of specific mRNPs in myoblasts and myotubes was investigated. -- mRNPs in polysomal arrays were primarily associated with the cytoskeleton. In addition, the cytoskeletal fraction also contained mRNA in the form of free mRNPs. Therefore, the association of mRNA with the cytoskeleton did not seem to depend on the presence of ribosomes for attachment. Furthermore, analysis of specific mRNAs in the various subcellular fractions of myoblasts and myotubes revealed differences in the distribution pattern of these mRNAs. -- The effects of depolymerizing the microfilaments with cytochalasin B in myoblasts, was investigated. Treatment of myoblasts with cytochalasin B did not result in movement of ribosomes or specific mRNPs from the cytoskeletal fraction to the soluble fraction. This indicates that in L6 myoblasts, ribosomes and mRNPs are not associated with microfilaments. In addition, it was observed that cytochalasin B inhibited the incorporation of precursor into RNA and not protein. The effect on RNA synthesis, however, was due to an inhibition of uptake of precursor uridine, which was found to be reversible.

Item Type: Thesis (Masters)
URI: http://research.library.mun.ca/id/eprint/5664
Item ID: 5664
Additional Information: Bibliography: leaves 75-84.
Department(s): Medicine, Faculty of
Date: 1986
Date Type: Submission
Library of Congress Subject Heading: Cytoskeleton; Cell compartmentation; Proteins--Synthesis
Medical Subject Heading: Cell Compartmentation; Cytoskeleton; RNA, Messenger

Actions (login required)

View Item View Item

Downloads

Downloads per month over the past year

View more statistics