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. 2008 May 22;27(11):1622–1632. doi: 10.1038/emboj.2008.89

Figure 7.

Figure 7

Model of the passage of nascent polypeptides through TF. TF directs the nascent chains through its interior in a sequential and length-dependent manner. (A) Initially (with a length of 40–60 aa), the N terminus of the nascent chain slides along the N domain, where it might be accessible by means of the lateral openings from both sides for processing factors such as PDF, MAP or SRP. (B) Up to a length of 90 aa, the nascent chain traverses through the C-terminal arms towards the PPIase domain and engages the entire interior. (C) Upon further elongation, the nascent chain might leave TF or, alternatively, may accumulate and perhaps fold in the interior of the TF chaperone. On demand, the folding of a subset of newly synthesized proteins is further assisted by cytosolic chaperones.