REL1 (TbMP52, RNA-editing ligase 1) — Trypanosoma brucei TREU927 — curation notes
Automated deep research was unavailable in this environment (Falcon auth failure, invalid OpenAI key). These notes are a manual literature review based on the UniProt record (P86927), the cached publications cited in GOA, and additional primary papers located by web search and verified against PubMed before caching.
Identity
- UniProt P86927 (RLGM1_TRYB2), 469 aa, gene REL1, synonym MP52 / TbMP52, TriTrypDB Tb927.9.4360. N-terminal mitochondrial transit peptide 1..44 (UniProt FT TRANSIT). Belongs to the RNA ligase 2 (Rnl2) family (InterPro IPR012647 RNA_lig_RNL2), the nucleotidyltransferase superfamily shared with DNA ligases and mRNA capping enzymes; active-site lysine K87 forms the covalent ligase-AMP intermediate.
- Paralog REL2 (TbMP48) sits in the insertion subcomplex; REL1 sits in the deletion subcomplex.
Function
Localization
- Mitochondrion (transit peptide; editosome purified from mitochondria PMID:11134327). MitoCarta SVM prediction PMID:20660476.
- TrypTag (GO_REF:0000109) gave kinetoplast and cytoplasm calls. Cytoplasm in GO includes the mitochondrion, so it is true but uninformative; a cytosolic signal could also be an N-terminal-tag artefact masking the transit peptide. Kinetoplast (sub-mitochondrial region around kDNA) is plausible given editing of maxicircle transcripts but the core site is the mitochondrial matrix.
- Complex map: REL1 was the bait in a TEV-elution pulldown PMID:26991453; PMID:26991453.
Curation decisions (summary)
- Ligase activity (IEA) -> MODIFY to RNA ligase (ATP) activity GO:0003972 (already present; experimentally supported).
- RNA modification (IDA, IEA) -> MODIFY to mitochondrial mRNA modification GO:0080156 (OLS-verified; child of mRNA modification and mitochondrial RNA modification). GO merged "RNA editing" into "RNA modification"; U-insertion/deletion editing has no dedicated term.
- Cytoplasm (TrypTag IDA) -> MODIFY to mitochondrion.
- Editosome GO:0031019, mitochondrion, RNA ligase (ATP) activity -> ACCEPT. Kinetoplast -> KEEP_AS_NON_CORE. ATP binding -> KEEP_AS_NON_CORE.
- Protist checks: no animal/plant-only terms; no host-process terms; no paralog over-annotation (REL1 vs REL2 subcomplex distinction is not represented in GO and needs no term).