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Cell-free translation systems have figured out more than one topologic form[7], [8], one of which appears to be fully translocated into the ER lumen, termed the secretory form (Sec-PrP).
As a result the fusion protein will be fully translocated and end up inside the secretory pathway.
Remarkably, in cells with fully translocated daughter chloroplasts, the YFP fluorescence extended to the cell division plane between the two daughter chloroplasts and resembled dot-like signals.
The construct with the conventional signal peptide is fully translocated into the secretory pathway, and hence separated from the PI3P patch-associated PEXEL proteins.
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In addition, PC1/3 does not have the traditional transmembrane segment and is thought to fully translocate into the ER lumen.
Tat substrates are produced with distinctive N-terminal signal peptides and are translocated as fully folded proteins.
The twin-arginine translocation (Tat) pathway is an unusual system that acts to translocate fully folded proteins across the bacterial plasma membrane, and the chloroplast thylakoid membrane [1 3].
Prokaryotic preproteins with an N-terminal twin-arginine (RR) motif-containing leader peptide are translocated in a fully folded state by the twin-arginine translocation (Tat) system.
In contrast to the Sec pathway, the Tat secretion system is able to translocate fully folded proteins across bacterial membranes [ 32 ].
Any gene residing in the subtelomeres or translocated to these loci acquires either fully silenced or fully active state.
The TAT system is distinguished by the ability to translocate fully-folded proteins and is found also in C. eutropha H16, C. metallidurans CH34, and R. solanacearum GMI1000.
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