{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T15:47:41Z","timestamp":1792165661994,"version":"4.4.0"},"reference-count":74,"publisher":"Cold Spring Harbor Laboratory","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["RNA"],"accepted":{"date-parts":[[2026,7,27]]},"published-print":{"date-parts":[[2026,11]]},"abstract":"<jats:p>\n                    Small regulatory RNAs (sRNAs) can specifically bind to their target mRNAs to inhibit their expression, either by promoting degradation or by blocking translation. However, the molecular determinants that select which repression mode an sRNA employs remain poorly understood. To investigate this, we used the model target mRNA\n                    <jats:italic>hdeD<\/jats:italic>\n                    , which is repressed by two sRNAs, CyaR and RprA, both of which use distinct modes of repression. Whereas CyaR promotes the target mRNA\n                    <jats:italic>hdeD<\/jats:italic>\n                    degradation, the sRNA RprA specifically blocks\n                    <jats:italic>hdeD<\/jats:italic>\n                    translation initiation, leaving\n                    <jats:italic>hdeD<\/jats:italic>\n                    mRNA intact. We found that mutating two nucleotides in the seed pairing region of RprA with\n                    <jats:italic>hdeD<\/jats:italic>\n                    is sufficient to switch its mode of repression from translation inhibition to degradation by recruiting RNase E. We investigated this further by using various RNase E deletion mutants of the C-terminal domain (CTD). Among these was an RNase E mutant deleted to contain a minimal C-terminal scaffold (\n                    <jats:italic>rne<\/jats:italic>\n                    701), a form which typically fails to promote sRNA-induced mRNA degradation. Our data indicated that even with a minimal scaffold, the mutated RprA sRNA still promoted\n                    <jats:italic>hdeD<\/jats:italic>\n                    mRNA degradation, whereas the native sRNA CyaR could not. Our data suggested that the mutated RprA sRNA relies primarily on the arginine-rich RNA-binding (ARRBD) domain of RNase E to induce target mRNA\n                    <jats:italic>hdeD<\/jats:italic>\n                    degradation. This suggests that the mutated RprA sRNA requires fewer components of the CTD of RNase E and RNA degradosome to induce target mRNA degradation.\n                  <\/jats:p>","DOI":"10.1261\/rna.080914.125","type":"journal-article","created":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T18:00:16Z","timestamp":1787248816000},"page":"1749-1764","source":"Crossref","is-referenced-by-count":0,"title":["Seed pairing between a small regulatory RNA and target mRNA determines cleavage by an RNase E with a minimal C-terminal scaffold"],"prefix":"10.1261","volume":"32","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8424-1685","authenticated-orcid":false,"given":"Carlos 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