PMID:16359675
| Citation |
Tomic, S, Johnson, AE, Hartl, FU and Etchells, SA (2006) Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains. FEBS Lett. 580:72-6 |
|---|---|
| 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 approximately 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 alpha-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. |
| Links |
PubMed Online version:10.1016/j.febslet.2005.11.050 |
| Keywords |
Animals; Cell-Free System/chemistry; Cell-Free System/metabolism; Chaperonins/chemistry; Chaperonins/metabolism; Cross-Linking Reagents/chemistry; Escherichia coli/chemistry; Escherichia coli/physiology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrophobic and Hydrophilic Interactions; Luciferases/biosynthesis; Luciferases/chemistry; Mice; Peptides/chemistry; Peptides/metabolism; Peptidylprolyl Isomerase/chemistry; Peptidylprolyl Isomerase/metabolism; Protein Binding/physiology; Protein Biosynthesis/physiology; Ribosomes/chemistry; Ribosomes/metabolism; alpha-Synuclein/biosynthesis; alpha-Synuclein/chemistry |
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