At the membrane frontier: A prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl-phosphates
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Imperiali_At the membrane.pdf
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1.02 MB
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Checksum (MD5)
58261b20106b06991fdad4c4c5a37b1c
Author(s)
Hartley, Meredith D.
Imperiali, Barbara
Date Issued
November 2011
Journal
Archives of Biochemistry and Biophysics
Publisher
Elsevier
Citation
Hartley, Meredith D., and Barbara Imperiali. “At the Membrane Frontier: A Prospectus on the Remarkable Evolutionary Conservation of Polyprenols and Polyprenyl-Phosphates.” Archives of Biochemistry and Biophysics 517, no. 2 (January 2012): 83–97.
Version
Author's final manuscript
Abstract
Long-chain polyprenols and polyprenyl-phosphates are ubiquitous and essential components of cellular membranes throughout all domains of life. Polyprenyl-phosphates, which include undecaprenyl-phosphate in bacteria and the dolichyl-phosphates in archaea and eukaryotes, serve as specific membrane-bound carriers in glycan biosynthetic pathways responsible for the production of cellular structures such as N-linked protein glycans and bacterial peptidoglycan. Polyprenyl-phosphates are the only form of polyprenols with a biochemically-defined role; however, unmodified or esterified polyprenols often comprise significant percentages of the cellular polyprenol pool. The strong evolutionary conservation of unmodified polyprenols as membrane constituents and polyprenyl-phosphates as preferred glycan carriers in biosynthetic pathways is poorly understood. This review surveys the available research to explore why unmodified polyprenols have been conserved in evolution and why polyprenyl-phosphates are universally and specifically utilized for membrane-bound glycan assembly.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution-Noncommercial-NoDerivatives
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DOI of Published Version
https://doi.org/10.1016/j.abb.2011.10.018
