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10.1038/s41467-025-67330-2 http://scihub22266oqcxt.onion/10.1038/s41467-025-67330-2 41390511!?!41390511 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=41390511&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 500 Internal Server Error in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Nat+Commun 2025 ; ? (?): ? Nephropedia Template TP {{tp|p=41390511|t=2025. Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation |pdf=|usr=}}{{41390511}} gab.com Text Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=41390511 #FOAvip In many bacterial species, transcription and translation can be coupled physically, with potential impact on the rates and efficiency of gene expression. Here, we present structural evidence from cryo-EM demonstrating that a bacterial RNA polymerase that is paused proximally to the promoter can associate with the pioneering 30S translation initiation complex (30S IC). These findings suggest that the physical link between transcription and translation can be established prior to commitment to protein synthesis. Although the mRNA is embedded in this 'early expressome' complex, it can nonetheless interact with small regulatory RNA (sRNA) and be targeted for cleavage in the protein-coding region by the RNA degradosome assembly in vitro. The potential tagging of transcripts with sRNA during pioneering and subsequent stages of translation initiation, when the 30S IC is at the 5' end of a polyribosome, may in principle contribute to efficient and rapid termination of gene expression in response to regulatory signals. Twit Text FOAVip Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=41390511 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=41390511 #FOAvip English Wikipedia <ref>{{Cite pmid|41390511}}</ref> Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation #MMPMID41390511 Roske JJ; Paris G; Goyal A; Rodnina M; Zenkin N; Bandyra KJ; Luisi BF Nat Commun 2025[Dec]; ? (?): ? PMID41390511show ga In many bacterial species, transcription and translation can be coupled physically, with potential impact on the rates and efficiency of gene expression. Here, we present structural evidence from cryo-EM demonstrating that a bacterial RNA polymerase that is paused proximally to the promoter can associate with the pioneering 30S translation initiation complex (30S IC). These findings suggest that the physical link between transcription and translation can be established prior to commitment to protein synthesis. Although the mRNA is embedded in this 'early expressome' complex, it can nonetheless interact with small regulatory RNA (sRNA) and be targeted for cleavage in the protein-coding region by the RNA degradosome assembly in vitro. The potential tagging of transcripts with sRNA during pioneering and subsequent stages of translation initiation, when the 30S IC is at the 5' end of a polyribosome, may in principle contribute to efficient and rapid termination of gene expression in response to regulatory signals. ?Structure of the 30S translation initiation complex coupled to paused (epmc).pdf DeepDyve Pubget Overpricing