Elsevier

Journal of Structural Biology

Volume 104, Issues 1–3, July–September 1990, Pages 38-43
Journal of Structural Biology

Bacteriophages M13 and Pf3 tell us how proteins insert into the membrane

https://doi.org/10.1016/1047-8477(90)90055-HGet rights and content

First page preview

First page preview
Click to open first page preview

References (24)

  • N. Kusukawa et al.

    EMBO J

    (1989)
  • A.A. Laminet et al.

    EMBO J

    (1990)
  • G.I. V. Heijne

    Eur. J. Biochem

    (1983)
  • P. Wolfe et al.

    J. Biol. Chem

    (1985)
  • D. Zilberstein et al.

    J. Bacteriol

    (1984)
  • L. Brundage et al.

    Cell

    (1990)
  • L.A. Day et al.

    Annu. Rev. Biophys. Biophys. Chem

    (1988)
  • M. Dürrenberger et al.
  • A. Gallusser et al.

    EMBO J

    (1990)
  • A. Kuhn

    Science

    (1987)
  • A. Kuhn

    Eur. J. Biochem

    (1988)
  • A. Kuhn et al.

    Nature (London)

    (1986)
  • Cited by (26)

    • YidC: A Protein with Multiple Functions in Bacterial Membrane Biogenesis

      2007, Enzymes
      Citation Excerpt :

      On the other hand, Alb3.1 is not essential for the cell [26] but is required for the efficient assembly of photosystem II and for maintaining thylakoid membrane levels of LHCB [27]. The most extensively studied proteins that are inserted by the Sec-independent YidC pathway in bacteria are the M13 phage procoat protein and Pf3 coat protein (for review see [28]). Procoat is synthesized with a leader sequence and contains one transmembrane segment in the 50-residue mature domain of the protein.

    • The role of lipids in membrane insertion and translocation of bacterial proteins

      2004, Biochimica et Biophysica Acta - Molecular Cell Research
    • Protein-lipid interactions of bacteriophage M13 major coat protein

      2003, Biochimica et Biophysica Acta - Biomembranes
      Citation Excerpt :

      Alternatively, the major coat protein can be incorporated in the membrane as a newly synthesised coat protein with an additional signal sequence consisting of 23 amino acid residues [27,28]. Charged residues and their interactions with the lipids [29–31] affect the membrane insertion of the newly synthesised precursor coat protein. After being inserted the signal sequence is cleaved off by the bacterial leader peptidase.

    View all citing articles on Scopus
    View full text