Figure 1: Overiew of translational block of the trp operon in B. subtilis by tryptophan RNA-binding attenuation protein (TRAP). | Nature Communications

Figure 1: Overiew of translational block of the trp operon in B. subtilis by tryptophan RNA-binding attenuation protein (TRAP).

From: Enhancing titres of therapeutic viral vectors using the transgene repression in vector production (TRiP) system

Figure 1

(i) TRAP is an 8 kDa protein that associates into a homomeric, torroidal ring comprising 11 TRAP monomers. The trp operon RNA leader contains a TRAP binding sequence (tbs) of KAG repeats separated by two/three, or infrequently more than three spacing nucleotides that contribute to secondary structure within the leader; this results in exposure of the Shine–Dalgarno (SD) sequence and consequently efficient translation of the trp operon mRNA. When L-tryptophan is present in excess, each of the 11 TRAP monomers binds L -tryptophan resulting in a conformational change on the outside of the 11-mer ring such that it can bind tightly to the tbs. This re-orders the secondary structure within the leader, causing the SD to become unavailable leading to attenuation of translation initiation. (ii) The TRAP-tbs configuration used by Nie and Htun to exemplify a RNA-binding protein-identification screen20, and in this study for blocking of transgene translation in viral vector production cells.

Back to article page