N-terminal lysines are essential for protein translocation via a modified ERAD system in complex plastids.

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  • Author(s): Lau JB;Lau JB; Stork S; Moog D; Sommer MS; Maier UG
  • Source:
    Molecular microbiology [Mol Microbiol] 2015 May; Vol. 96 (3), pp. 609-20. Date of Electronic Publication: 2015 Mar 11.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Scientific Publications Country of Publication: England NLM ID: 8712028 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1365-2958 (Electronic) Linking ISSN: 0950382X NLM ISO Abbreviation: Mol Microbiol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Oxford, OX ; Boston, MA : Blackwell Scientific Publications, c1987-
    • Subject Terms:
      Protein Transport*; Algal Proteins/*metabolism ; Mucoproteins/*metabolism ; Plastids/*metabolism ; Rhodophyta/*metabolism; Intracellular Membranes/metabolism ; Models, Biological
    • Abstract:
      Nuclear-encoded pre-proteins being imported into complex plastids of red algal origin have to cross up to five membranes. Thereby, transport across the second outermost or periplastidal membrane (PPM) is facilitated by SELMA (symbiont-specific ERAD-like machinery), an endoplasmic reticulum-associated degradation (ERAD)-derived machinery. Core components of SELMA are enzymes involved in ubiquitination (E1-E3), a Cdc48 ATPase complex and Derlin proteins. These components are present in all investigated organisms with four membrane-bound complex plastids of red algal origin, suggesting a ubiquitin-dependent translocation process of substrates mechanistically similar to the process of retro-translocation in ERAD. Even if, according to the current model, translocation via SELMA does not end up in the classical poly-ubiquitination, transient mono-/oligo-ubiquitination of pre-proteins might be required for the mechanism of translocation. We investigated the import mechanism of SELMA and were able to show that protein transport across the PPM depends on lysines in the N-terminal but not in the C-terminal part of pre-proteins. These lysines are predicted to be targets of ubiquitination during the translocation process. As proteins lacking the N-terminal lysines get stuck in the PPM, a 'frozen intermediate' of the translocation process could be envisioned and initially characterized.
      (© 2015 John Wiley & Sons Ltd.)
    • Accession Number:
      0 (Algal Proteins)
      0 (Mucoproteins)
      0 (lysin, gastropoda)
    • Publication Date:
      Date Created: 20150204 Date Completed: 20160111 Latest Revision: 20160308
    • Publication Date:
      20221213
    • Accession Number:
      10.1111/mmi.12959
    • Accession Number:
      25644868