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Identification of regulatory targets for the bacterial Nus factor complex

Gabriele Baniulyte, Navjot Singh, Courtney Benoit, Richard Johnson, Robert Ferguson, Mauricio Paramo, Anne M. Stringer, Ashley Scott, Pascal Lapierre and Joseph T. Wade ()
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Gabriele Baniulyte: New York State Department of Health
Navjot Singh: New York State Department of Health
Courtney Benoit: New York State Department of Health
Richard Johnson: New York State Department of Health
Robert Ferguson: New York State Department of Health
Mauricio Paramo: New York State Department of Health
Anne M. Stringer: New York State Department of Health
Ashley Scott: New York State Department of Health
Pascal Lapierre: New York State Department of Health
Joseph T. Wade: New York State Department of Health

Nature Communications, 2017, vol. 8, issue 1, 1-8

Abstract: Abstract Nus factors are broadly conserved across bacterial species, and are often essential for viability. A complex of five Nus factors (NusB, NusE, NusA, NusG and SuhB) is considered to be a dedicated regulator of ribosomal RNA folding, and has been shown to prevent Rho-dependent transcription termination. Here, we identify an additional cellular function for the Nus factor complex in Escherichia coli: repression of the Nus factor-encoding gene, suhB. This repression occurs primarily by translation inhibition, followed by Rho-dependent transcription termination. Thus, the Nus factor complex can prevent or promote Rho activity depending on the gene context. Conservation of putative NusB/E binding sites upstream of Nus factor genes suggests that Nus factor autoregulation occurs in many bacterial species. Additionally, many putative NusB/E binding sites are also found upstream of other genes in diverse species, and we demonstrate Nus factor regulation of one such gene in Citrobacter koseri. We conclude that Nus factors have an evolutionarily widespread regulatory function beyond ribosomal RNA, and that they are often autoregulatory.

Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-02124-9

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DOI: 10.1038/s41467-017-02124-9

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