Year: 2014
Type: article
Abstract: In bacteria, protein synthesis can be coupled to transcription, but in eukaryotes it is believed to occur solely in the cytoplasm. Using pulses as short as 5 s, we find that three analogues--L-azidohomoalanine, puromycin (detected after attaching fluors using 'click' chemistry or immuno-labeling), and amino acids tagged with 'heavy' 15N and 13C (detected using secondary ion mass spectrometry)--are incorporated into the nucleus and cytoplasm in a process sensitive to translational inhibitors. The nuclear incorporation represents a significant fraction of the total, and labels in both compartments have half-lives of less than a minute; results are consistent with most newly-made peptides being destroyed soon after they are made. As nascent RNA bearing a premature termination codon (detected by fluorescence in situ hybridization) is also eliminated by a mechanism sensitive to a translational inhibitor, the nuclear turnover of peptides is probably a by-product of proof-reading the RNA for stop codons (a process known as nonsense-mediated decay). We speculate that the apparently-wasteful turnover of this previously-hidden ('dark-matter') world of peptide is involved in regulating protein production.
Source: PLoS ONE
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,382
Awards: G2251270888, G2463466672, G295399147, G3038452519, Engineering stable calibration standards for biomedical research, Dissecting the mechanism by which glycosyltransferases calalyse mannosyl transfer, G7739863634, The CHELL : A Bottom-Up approach to in vitro and in silico Minimal Life-like Constructs, Creating a Synthetic Platform for Understanding and Exploiting Glycoconjugates, Advanced Microscopy for Chromosome and RNA Dynamics., Zirconium alloys for high burn-up fuel in current and advanced light water-cooled reactors, G8603049439
OpenAlex ID: W2154809063