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Title | The missing part: the Archaeoglobus fulgidus Argonaute forms a functional heterodimer with an N-L1-L2 domain protein. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 52, Issue 5, Page 2530-2545, Year 2024 |
Publish date | Mar 21, 2024 |
Authors | Elena Manakova / Edvardas Golovinas / Reda Pocevičiūtė / Giedrius Sasnauskas / Arunas Silanskas / Danielis Rutkauskas / Marija Jankunec / Evelina Zagorskaitė / Edvinas Jurgelaitis / Algirdas Grybauskas / Česlovas Venclovas / Mindaugas Zaremba |
PubMed Abstract | Argonaute (Ago) proteins are present in all three domains of life (bacteria, archaea and eukaryotes). They use small (15-30 nucleotides) oligonucleotide guides to bind complementary nucleic acid ...Argonaute (Ago) proteins are present in all three domains of life (bacteria, archaea and eukaryotes). They use small (15-30 nucleotides) oligonucleotide guides to bind complementary nucleic acid targets and are responsible for gene expression regulation, mobile genome element silencing, and defence against viruses or plasmids. According to their domain organization, Agos are divided into long and short Agos. Long Agos found in prokaryotes (long-A and long-B pAgos) and eukaryotes (eAgos) comprise four major functional domains (N, PAZ, MID and PIWI) and two structural linker domains L1 and L2. The majority (∼60%) of pAgos are short pAgos, containing only the MID and inactive PIWI domains. Here we focus on the prokaryotic Argonaute AfAgo from Archaeoglobus fulgidus DSM4304. Although phylogenetically classified as a long-B pAgo, AfAgo contains only MID and catalytically inactive PIWI domains, akin to short pAgos. We show that AfAgo forms a heterodimeric complex with a protein encoded upstream in the same operon, which is a structural equivalent of the N-L1-L2 domains of long pAgos. This complex, structurally equivalent to a long PAZ-less pAgo, outperforms standalone AfAgo in guide RNA-mediated target DNA binding. Our findings provide a missing piece to one of the first and the most studied pAgos. |
External links | Nucleic Acids Res / PubMed:38197228 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.4 - 3.43 Å |
Structure data | EMDB-17973, PDB-8pvv: EMDB-18386, PDB-8qg0: PDB-8ok9: PDB-8old: PDB-8olj: |
Chemicals | ChemComp-MG: ChemComp-ACY: ChemComp-EDO: ChemComp-PEG: ChemComp-HOH: ChemComp-CAC: ChemComp-CL: ChemComp-MPD: ChemComp-NA: ChemComp-GOL: ChemComp-IPA: ChemComp-K: ChemComp-TRS: |
Source |
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Keywords | RNA BINDING PROTEIN / Protein-nucleic acid interactions / Argonaute / pAgo / guide and target specificity / PROTEIN BINDING / DNA BINDING PROTEIN / PIWI DOMAIN / PROTEIN-DNA COMPLEX |