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Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains
Author(s) -
Tomic Sladjana,
Johnson Arthur E.,
Hartl F. Ulrich,
Etchells Stephanie A.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.050
Subject(s) - polypeptide chain , ribosome , chemistry , chaperone (clinical) , protease , biophysics , biochemistry , microbiology and biotechnology , biology , rna , enzyme , medicine , pathology , gene
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.