| Literature DB >> 28977553 |
Haitian Fan1, Adam B Conn1, Preston B Williams2, Stephen Diggs1, Joseph Hahm1, Howard B Gamper3, Ya-Ming Hou3, Seán E O'Leary1, Yinsheng Wang2, Gregor M Blaha1.
Abstract
In prokaryotes, RNA polymerase and ribosomes can bind concurrently to the same RNA transcript, leading to the functional coupling of transcription and translation. The interactions between RNA polymerase and ribosomes are crucial for the coordination of transcription with translation. Here, we report that RNA polymerase directly binds ribosomes and isolated large and small ribosomal subunits. RNA polymerase and ribosomes form a one-to-one complex with a micromolar dissociation constant. The formation of the complex is modulated by the conformational and functional states of RNA polymerase and the ribosome. The binding interface on the large ribosomal subunit is buried by the small subunit during protein synthesis, whereas that on the small subunit remains solvent-accessible. The RNA polymerase binding site on the ribosome includes that of the isolated small ribosomal subunit. This direct interaction between RNA polymerase and ribosomes may contribute to the coupling of transcription to translation.Entities:
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Year: 2017 PMID: 28977553 PMCID: PMC5737488 DOI: 10.1093/nar/gkx719
Source DB: PubMed Journal: Nucleic Acids Res ISSN: 0305-1048 Impact factor: 16.971