Abstract:
:Polypeptide chains synthesized by membrane-bound ribosomes are translocated through, and integrated into, the endoplasmic reticulum (ER) membrane by means of the protein translocation channel, the translocon. Positive charges on the nascent chain determine the orientation of the hydrophobic segment as it is inserted into the translocon and enhance the stop-translocation of translocating hydrophobic segments. Here we show that positive charges temporarily arrested ongoing polypeptide chain movement through the ER translocon by electrostatic interaction, even in the absence of a hydrophobic segment. The C-terminus of the polypeptide chain was elongated during the arrest, and then the full-length polypeptide chain moved through the translocon. The translocation-arrested polypeptide was not anchored to the membrane and the charges were on the cytoplasmic side of the membrane. The arrest effect was prevented by negatively charged residues inserted into the positive-charge cluster, and it was also suppressed by high salt conditions. We propose that positive charges are independent translocation regulators that are more active than previously believed.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Fujita H,Yamagishi M,Kida Y,Sakaguchi Mdoi
10.1242/jcs.086850subject
Has Abstractpub_date
2011-12-15 00:00:00pages
4184-93issue
Pt 24eissn
0021-9533issn
1477-9137pii
jcs.086850journal_volume
124pub_type
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