Polysome

A polyribosome (or polysome or ergasome) is a complex of an mRNA molecule and two or more ribosomes that act to translate mRNA instructions into polypeptides. Originally coined "ergosomes" in 1963, they were further characterized by Jonathan Warner, Paul M. Knopf,[1] and Alex Rich. The simultaneous analysis of the polysome with all the peptides it produces under given conditions (the translatome) lead to a better insight of the complexity of how mutations, extracellular stimuli, intercellular cues, growth conditions, and stress could lead to the change of translation in the cell. Polysomes consist of varying numbers of ribosomes, and each ribosome contributes to the addition of its substantial mass. They act as a platform for signalling molecules to get involved in the emergence of polypeptides and ribosomes, and aid the nascent polypeptides to fold in the presence of chaperones, which later impact on the function of synthesized polysomes.

Structure

Atomic-force microscopy (AFM) was used to obtain the images of polysomes from mouse brain samples in air and liquid. The images were then reconstructed to depict structures in three-dimensions, thereby facilitating the study into how polysomes are organized. Polysomes can be directly visualized by electron microscopy because they form very high molecular weight particles. Many ribosomes simultaneously read one mRNA polypeptide by progressing along the mRNA chain to synthesize the same protein. They may appear as linear polysomes or circular rosettes with microscopy, but are mainly circular in vivo. This circularization is aided by the fact that mRNA is able to be twisted into a circular formation, allowing a cycle of rapid ribosome recycling to occur. The 5' 7-methylguanosine cap and 3' poly(A) tail present on eukaryotic mRNA aid in this process.

Types of Polysome

Polyribosomes can be found in two forms: free and membrane bound. The two forms differ by the poly(A) and non-poly(A) protein binding sequence.

References
  1. Cambra, Kris (Spring 2017). "Paul M. Knopf, PhD". Brown Medicine. Brown University. Retrieved 24 July 2017.
  • Michael M. Cox; Jennifer A. Doudna; Michael O'Donnell (July 2011). Molecular Biology: Principles and Practice. Macmillan Higher Education. ISBN 978-1-4292-9273-3.
  • Staehelin, T.; Brinton, C. C.; Wettstein, F. O.; Noll, H. (1963). "Structure and Function of E. Coli Ergosomes". Nature. 199 (4896): 865–870. doi:10.1038/199865a0 ISSN 0028-0836.
  • Warner JR, Knopf PM, Rich A (1963). "A multiple ribosomal structure in protein synthesis". Proc. Natl. Acad. Sci. U.S.A. 49: 122–129. Bibcode: 1963PNAS...49..122W. doi:10.1073/pnas.49.1.122 PMID 13998950.
  • Harvey Lodish (1999). "4.5. Stepwise Formation of Proteins on Ribosomes". Molecular cell biology. New York: Scientific American Books. ISBN 0-7167-3136-3.
  • Brielle, Régine; Pinel-Marie, Marie-Laure; Chat, Sophie; Gillet, Reynald; Felden, Brice. "Purification, identification, and functional analysis of polysomes from the human pathogen Staphylococcus aureus". Methods. doi:10.1016/j.ymeth.2016.10.003
  • Qin, Daoming; Fredrick, Kurt. "Chapter Eight - Analysis of Polysomes from Bacteria". Methods in Enzymology. Academic Press. pp. 159–172.
  • Gandin, Valentina; Sikström, Kristina; Alain, Tommy; Morita, Masahiro; McLaughlan, Shannon; Larsson, Ola; Topisirovic, Ivan (17 May 2014). "Polysome Fractionation and Analysis of Mammalian Translatomes on a Genome-wide Scale". Journal of Visualized Experiments : JoVE (87). doi:10.3791/51455 ISSN 1940-087X PMID 8035778.
  • Moss, R.; Pryme, I. F.; Vedeler, A. (23 February 1994). "Free, cytoskeletal-bound and membrane-bound polysomes isolated from MPC-11 and Krebs II ascites cells differ in their complement of poly(A) binding proteins". Molecular and Cellular Biochemistry. 131 (2): 131–139. ISSN 0300-8177 PMID 8035778.
  • Lunelli, Lorenzo; Bernabò, Paola; Bolner, Alice; Vaghi, Valentina; Marchioretto, Marta; Viero, Gabriella (16 March 2016). "Peering at Brain Polysomes with Atomic Force Microscopy". Journal of Visualized Experiments (109). doi:10.3791/53851 ISSN 1940-087X.
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