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  • 1.
    Farias-Rico, Jose Arcadio
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Ruud Selin, Frida
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Myronidi, Ioanna
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Fruehauf, Marie
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    von Heijne, Gunnar
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
    Effects of protein size, thermodynamic stability, and net charge on cotranslational folding on the ribosome2018In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 115, no 40, p. e9280-E9287Article in journal (Refereed)
    Abstract [en]

    During the last five decades, studies of protein folding in dilute buffer solutions have produced a rich picture of this complex process. In the cell, however, proteins can start to fold while still attached to the ribosome (cotranslational folding) and it is not yet clear how the ribosome affects the folding of protein domains of different sizes, thermodynamic stabilities, and net charges. Here, by using arrest peptides as force sensors and on-ribosome pulse proteolysis, we provide a comprehensive picture of how the distance from the peptidyl transferase center in the ribosome at which proteins fold correlates with protein size. Moreover, an analysis of a large collection of mutants of the Escherichia coli ribosomal protein 56 shows that the force exerted on the nascent chain by protein folding varies linearly with the thermodynamic stability of the folded state, and that the ribosome environment disfavors folding of domains of high net-negative charge.

  • 2.
    Ring, Andreas
    et al.
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Myronidi, Ioanna
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Ljungdahl, Per O.
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    The ER membrane chaperone Shr3 co-translationally assists biogenesis of related polytopic membrane protein substratesManuscript (preprint) (Other academic)
    Abstract [en]

    Polytopic membrane proteins with multiple transmembrane segments (TMS) co-translationally insert into the endoplasmic reticulum (ER) membrane of eukaryotic cells. Discrete sets of polytopic membrane proteins in Saccharomyces cerevisiae require ER membrane-localized chaperones (MLC) to prevent aggregation and fold properly. Shr3, the best characterized MLC, is specifically required for the functional expression of amino acid permeases (AAP), a family of transport proteins comprised of twelve TMS. We performed comprehensive scanning mutagenesis and deletion analysis of Shr3 combined with split-ubiquitin approaches to probe chaperone-substrate (Shr3-AAP) interactions in vivo. We report a surprisingly low level of sequence specificity underlies Shr3-AAP interactions, which initiate after the first 2 to 4 TMS of AAP partition into the membrane. The Shr3-AAP interactions successively strengthen and then weaken as all 12 TMS are inserted. Thus, Shr3 acts transiently in a co-translationally manner to prevent TMS of translation intermediates from engaging in non-productive interactions, thereby preventing AAP misfolding during biogenesis.

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