Bacteriophages M13 and Pf3 tell us how proteins insert into the membrane
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Cited by (26)
Polarity and charge of the periplasmic loop determine the YidC and sec translocase requirement for the M13 procoat lep protein
2014, Journal of Biological ChemistryYidC: A Protein with Multiple Functions in Bacterial Membrane Biogenesis
2007, EnzymesCitation 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 ResearchProtein-lipid interactions of bacteriophage M13 major coat protein
2003, Biochimica et Biophysica Acta - BiomembranesCitation 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.
Δψ Stimulates membrane translocation of the C-terminal part of a signal sequence
1999, Journal of Biological ChemistryDirect evidence that the proton motive force inhibits membrane translocation of positively charged residues within membrane proteins
1999, Journal of Biological Chemistry