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Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.


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.

SUBMITTER: Fan H 

PROVIDER: S-EPMC5737488 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.

Fan Haitian H   Conn Adam B AB   Williams Preston B PB   Diggs Stephen S   Hahm Joseph J   Gamper Howard B HB   Hou Ya-Ming YM   O'Leary Seán E SE   Wang Yinsheng Y   Blaha Gregor M GM  

Nucleic acids research 20171101 19


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 form  ...[more]

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