Component
P-site peptidyl-tRNA
Independent rna record; interpretation is limited by each linked claim and its study context.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
Where it participates (unsigned role)
At the cytosolic 80S ribosome, the alpha-amino group of A-site lysyl-tRNA accepts the P-site nascent peptide, incorporating lysine into a peptide bond; the extended chain remains attached to the incoming tRNA.
Experimental context and source evidence
- experimental_model
- Human cell lysate translation products; rabbit reticulocyte ribosome-nascent-chain cryo-EM
- limitations
- AAG-coded translation controls directly show elongation. The structural experiment concerns poly(A)-dependent stalling; it does not establish a dietary deficiency response or instant release of the lysine-carrying tRNA.
- organism
- Homo sapiens and Oryctolagus cuniculus
- plain_language
- The ribosome adds charged lysine to a growing protein chain.
- primary_references
- [chandrasekaran2019] Mechanism of ribosome stalling during translation of a poly(A) tail (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6900289/ DOI: 10.1038/s41594-019-0331-x
- tissue_or_cell_type
- Cytosolic translation; cultured-cell lysate and reticulocyte lysate
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 347–355
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cell lysate translation products; rabbit reticulocyte ribosome-nascent-chain cryo-EM · source_derived_draft · unverified_draft
### ribosomal-lysine-incorporation At the cytosolic 80S ribosome, the alpha-amino group of A-site lysyl-tRNA accepts the P-site nascent peptide, incorporating lysine into a peptide bond; the extended chain remains attached to the incoming tRNA. Plain language: The ribosome adds charged lysine to a growing protein chain. Condition category: normal organism: Homo sapiens and Oryctolagus cuniculus tissue_or_cell_type: Cytosolic translation; cultured-cell lysate and reticulocyte lysate experimental_model: Human cell lysate translation products; rabbit reticulocyte ribosome-nascent-chain cryo-EM limitations: AAG-coded translation controls directly show elongation. The structural experiment concerns poly(A)-dependent stalling; it does not establish a dietary deficiency response or instant release of the lysine-carrying tRNA. [chandrasekaran2019] Mechanism of ribosome stalling during translation of a poly(A) tail (2019). https://pmc.ncbi.nlm.nih.gov/articles/PMC6900289/ DOI: 10.1038/s41594-019-0331-x
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.