Characterization of YlxR/Ssr1238, a conserved RNA binding protein in a model cyanobacterium

ABSTRACT: Throughout the tree of life RNA-binding proteins play important roles in the regulation of gene expression and RNA metabolism, but they are only poorly characterized in cyanobacteria. Here, we characterized the protein Ssr1238 from the model cyanobacterium Synechocystis sp. PCC 6803, which was predicted as a potential RNA-binding protein. Ssr1238 is a potential homolog of the protein YlxR from Bacillus subtilis and is encoded in a syntenic region within the nusA-ssr1238-infB operon. Co-immunoprecipitation of proteins followed by MS analysis and sequencing of UV-cross-linked co-immunoprecipitated RNA samples identified potential interaction partners of Ssr1238. The most highly enriched transcript was the RNase P RNA, while RnpA, the protein component of RNase P was among the most highly enriched proteins, consistent with recent findings that YlxR proteins can influence the enzymatic activity of RNase P. The data further suggest that Ssr1238 interacts with the 3 region of gene ssl3177, encoding a rare lipoprotein homolog and with the precursor transcript of the initiator tRNAfMet and the group I intron in it. Thus, Ssr1238 may play additional roles in the initiation of translation and cell division. The data also show a strong connection to the RNA maturation and modification system indicated by co-precipitation of riboendonuclease E, RNA methyltransferase Sll1967, the A-adding tRNA nucleotidyltransferase Sll1253 and queuine tRNA-ribosyltransferase, as well as enolase. Our results are consistent with recent findings that the B. subtilis YlxR protein functions as an RNase P modulator (RnpM), extend its proposed role to the phylum cyanobacteria and suggest additional functionalities.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Synechocystis Sp. Pcc 6803 (ncbitaxon:1148)

SUBMITTER: Wolfgang R. Hess  

PROVIDER: MSV000093645 | MassIVE | Tue Dec 12 04:17:00 GMT 2023

SECONDARY ACCESSION(S): PXD047746

REPOSITORIES: MassIVE