Reichelt, Robert and Rothmeier, Tamara and Gruenberger, Felix and Willkomm, Sarah and Bruckmann, Astrid and Hausner, Winfried and Grohmann, Dina (2023) The archaeal Lsm protein from Pyrococcus furiosus binds co-transcriptionally to poly(U)-rich target RNAs. BIOLOGICAL CHEMISTRY, 404 (11-12). pp. 1085-1100. ISSN 1431-6730, 1437-4315
Full text not available from this repository. (Request a copy)Abstract
Posttranscriptional processes in Bacteria include the association of small regulatory RNAs (sRNA) with a target mRNA. The sRNA/mRNA annealing process is often mediated by an RNA chaperone called Hfq. The functional role of bacterial and eukaryotic Lsm proteins is partially understood, whereas knowledge about archaeal Lsm proteins is scarce. Here, we used the genetically tractable archaeal hyperthermophile Pyrococcus furiosus to identify the protein interaction partners of the archaeal Sm-like proteins (PfuSmAP1) using mass spectrometry and performed a transcriptome-wide binding site analysis of PfuSmAP1. Most of the protein interaction partners we found are part of the RNA homoeostasis network in Archaea including ribosomal proteins, the exosome, RNA-modifying enzymes, but also RNA polymerase subunits, and transcription factors. We show that PfuSmAP1 preferentially binds messenger RNAs and antisense RNAs recognizing a gapped poly(U) sequence with high affinity. Furthermore, we found that SmAP1 co-transcriptionally associates with target RNAs. Our study reveals that in contrast to bacterial Hfq, PfuSmAP1 does not affect the transcriptional activity or the pausing behaviour of archaeal RNA polymerases. We propose that PfuSmAP1 recruits antisense RNAs to target mRNAs and thereby executes its putative regulatory function on the posttranscriptional level.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SM-LIKE PROTEINS; CRYSTAL-STRUCTURES; RIBOSOMAL-RNA; HFQ; COMPLEXES; POLYMERASE; EXOSOME; TERMINATION; DOMAIN; MOTIF; Sm-like protein; SmAP; RNA-binding protein; Archaea; RNA polymerase; transcription |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Gunter Meister Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Dina Grohmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Mar 2024 11:27 |
| Last Modified: | 07 Mar 2024 11:27 |
| URI: | https://pred.uni-regensburg.de/id/eprint/58895 |
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