Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052209 | FEBS Letters | 2006 | 5 Pages |
Abstract
Ribosome-bound trigger factor (TF) is the first chaperone encountered by a nascent polypeptide chain in bacteria. TF has been proposed to form a cradle-shaped shield for nascent chains up to ∼130 residues to fold in a protected environment upon exit from the ribosome. We report that nascent chains of luciferase up to 280 residues in length are relatively protected by TF against digestion by proteinase K. In contrast, nascent chains of the constitutively unstructured protein α-synuclein were not protected, although they were in close proximity to TF by crosslinking. Thus, TF is not a general shield for nascent chains. Protease protection appears to depend on a hydrophobic interaction of TF with nascent polypeptides.
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Authors
Sladjana Tomic, Arthur E. Johnson, F. Ulrich Hartl, Stephanie A. Etchells,