Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1: Membrane insertion of Rot1p

María Angeles Juanes, Carlos Andrés Martínez-garay, Juan Carlos Igual, María Carmen Bañó

    Research output: Contribution to journalArticle

    Abstract

    Rot1 is an essential yeast protein that has been related to cell wall biosynthesis, actin cytoskeleton dynamics and protein folding. Rot1 is an N-glycosylated protein anchored to the nuclear envelope–endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translocated to the ER by a post-translational mechanism. Here, we investigate the protein domain required to target and translocate Rot1 to the ER membrane. We found that several deletions of the N-terminal region of Rot1 prevented neither membrane targeting nor the insertion of this protein. Interestingly, we obtained the same results when different truncated forms in the C-terminal transmembrane domain were analyzed, suggesting the presence of an internal topogenic element that is capable of translocating Rot1 to the ER. To identify this sequence, we generated a combination of N- and C-terminal deletion mutants of Rot1 and we investigated their insertion into the membrane. The results show that two regions, amino acids 26–60 and 200–228, are involved in the post-translational translocation of Rot1 across the ER membrane.
    Original languageEnglish
    Pages (from-to)639-647
    JournalFEMS Yeast Research
    Volume10
    Issue number6
    DOIs
    Publication statusPublished - 1 Sep 2010

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