{"entity": "researcher", "timestamp": "2026-08-18T04:45:18.997Z", "family": "Ignatova", "given": "Zoya", "initials": "Z", "orcid": "0000-0002-9478-8825", "affiliations": [], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/15d0b4be02ca4c1884f0ad793462901c.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/15d0b4be02ca4c1884f0ad793462901c"}}, "publications": [{"entity": "publication", "iuid": "430c270305eb49f3a5e61581718ae6c7", "links": {"self": {"href": "https://publications.scilifelab.se/publication/430c270305eb49f3a5e61581718ae6c7.json"}, "display": {"href": "https://publications.scilifelab.se/publication/430c270305eb49f3a5e61581718ae6c7"}}, "title": "RqcH and RqcP catalyze processive poly-alanine synthesis in a reconstituted ribosome-associated quality control system.", "authors": [{"family": "Takada", "given": "Hiraku", "initials": "H"}, {"family": "Crowe-McAuliffe", "given": "Caillan", "initials": "C"}, {"family": "Polte", "given": "Christine", "initials": "C"}, {"family": "Sidorova", "given": "Zhanna Yu", "initials": "ZY"}, {"family": "Murina", "given": "Victoriia", "initials": "V"}, {"family": "Atkinson", "given": "Gemma C", "initials": "GC"}, {"family": "Konevega", "given": "Andrey L", "initials": "AL"}, {"family": "Ignatova", "given": "Zoya", "initials": "Z", "orcid": "0000-0002-9478-8825", "researcher": {"href": "https://publications.scilifelab.se/researcher/15d0b4be02ca4c1884f0ad793462901c.json"}}, {"family": "Wilson", "given": "Daniel N", "initials": "DN", "orcid": "0000-0003-3816-3828", "researcher": {"href": "https://publications.scilifelab.se/researcher/bd50ba35f7c74d7e9d4f42fbc49739f2.json"}}, {"family": "Hauryliuk", "given": "Vasili", "initials": "V", "orcid": "0000-0003-2389-5057", "researcher": {"href": "https://publications.scilifelab.se/researcher/17ea83b1d20f43f9872edbf89b275e5d.json"}}], "type": "journal article", "published": "2021-08-20", "journal": {"title": "Nucleic Acids Res.", "issn": "1362-4962", "issn-l": "0305-1048", "volume": "49", "issue": "14", "pages": "8355-8369"}, "abstract": "In the cell, stalled ribosomes are rescued through ribosome-associated protein quality-control (RQC) pathways. After splitting of the stalled ribosome, a C-terminal polyalanine 'tail' is added to the unfinished polypeptide attached to the tRNA on the 50S ribosomal subunit. In Bacillus subtilis, polyalanine tailing is catalyzed by the NEMF family protein RqcH, in cooperation with RqcP. However, the mechanistic details of this process remain unclear. Here we demonstrate that RqcH is responsible for tRNAAla selection during RQC elongation, whereas RqcP lacks any tRNA specificity. The ribosomal protein uL11 is crucial for RqcH, but not RqcP, recruitment to the 50S subunit, and B. subtilis lacking uL11 are RQC-deficient. Through mutational mapping, we identify critical residues within RqcH and RqcP that are important for interaction with the P-site tRNA and/or the 50S subunit. Additionally, we have reconstituted polyalanine-tailing in vitro and can demonstrate that RqcH and RqcP are necessary and sufficient for processivity in a minimal system. Moreover, the in vitro reconstituted system recapitulates our in vivo findings by reproducing the importance of conserved residues of RqcH and RqcP for functionality. Collectively, our findings provide mechanistic insight into the role of RqcH and RqcP in the bacterial RQC pathway.", "doi": "10.1093/nar/gkab589", "pmid": "34255840", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "6320412"}, {"db": "pmc", "key": "PMC8373112"}], "notes": [], "created": "2021-12-14T12:41:03.729Z", "modified": "2022-04-01T07:14:15.200Z"}, {"entity": "publication", "iuid": "2ba033fd1efc4e399b47b8681da72993", "links": {"self": {"href": "https://publications.scilifelab.se/publication/2ba033fd1efc4e399b47b8681da72993.json"}, "display": {"href": "https://publications.scilifelab.se/publication/2ba033fd1efc4e399b47b8681da72993"}}, "title": "Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP.", "authors": [{"family": "Crowe-McAuliffe", "given": "Caillan", "initials": "C"}, {"family": "Takada", "given": "Hiraku", "initials": "H"}, {"family": "Murina", "given": "Victoriia", "initials": "V"}, {"family": "Polte", "given": "Christine", "initials": "C"}, {"family": "Kasvandik", "given": "Sergo", "initials": "S"}, {"family": "Tenson", "given": "Tanel", "initials": "T"}, {"family": "Ignatova", "given": "Zoya", "initials": "Z", "orcid": "0000-0002-9478-8825", "researcher": {"href": "https://publications.scilifelab.se/researcher/15d0b4be02ca4c1884f0ad793462901c.json"}}, {"family": "Atkinson", "given": "Gemma C", "initials": "GC"}, {"family": "Wilson", "given": "Daniel N", "initials": "DN", "orcid": "0000-0003-3816-3828", "researcher": {"href": "https://publications.scilifelab.se/researcher/bd50ba35f7c74d7e9d4f42fbc49739f2.json"}}, {"family": "Hauryliuk", "given": "Vasili", "initials": "V", "orcid": "0000-0003-2389-5057", "researcher": {"href": "https://publications.scilifelab.se/researcher/17ea83b1d20f43f9872edbf89b275e5d.json"}}], "type": "journal article", "published": "2021-01-07", "journal": {"title": "Mol. Cell", "issn": "1097-4164", "issn-l": "1097-2765", "volume": "81", "issue": "1", "pages": "115-126.e7"}, "abstract": "In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal \"tails.\" How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit.", "doi": "10.1016/j.molcel.2020.11.002", "pmid": "33259810", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "S1097-2765(20)30780-2"}], "notes": [], "created": "2020-12-10T11:26:33.440Z", "modified": "2021-11-10T12:27:47.555Z"}]}