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Frontiers in microbiology
2020;11 588487.

The Partner Switching System of the SigF Sigma Factor in and Induction of the SigF Regulon Under Respiration-Inhibitory Conditions.

Yuna Oh, Su-Yeon Song, Hye-Jun Kim, Gil Han, Jihwan Hwang, Ho-Young Kang, Jeong-Il Oh
Author Information
  1. Yuna Oh: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
  2. Su-Yeon Song: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
  3. Hye-Jun Kim: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
  4. Gil Han: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
  5. Jihwan Hwang: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
  6. Ho-Young Kang: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
  7. Jeong-Il Oh: Department of Integrated Biological Science, Pusan National University, Busan, South Korea.
PMID: 33304334 DOI: 10.3389/fmicb.2020.588487

Abstract

The partner switching system (PSS) of the SigF regulatory pathway in has been previously demonstrated to include the anti-sigma factor RsbW (MSMEG_1803) and two anti-sigma factor antagonists RsfA and RsfB. In this study, we further characterized two additional RsbW homologs and revealed the distinct roles of three RsbW homologs [RsbW1 (MSMEG_1803), RsbW2 (MSMEG_6129), and RsbW3 (MSMEG_1787)] in the SigF PSS. RsbW1 and RsbW2 serve as the anti-sigma factor of SigF and the protein kinase phosphorylating RsfB, respectively, while RsbW3 functions as an anti-SigF antagonist through its protein interaction with RsbW1. Using relevant mutant strains, RsfB was demonstrated to be the major anti-SigF antagonist in . The phosphorylation state of Ser-63 was shown to determine the functionality of RsfB as an anti-SigF antagonist. RsbW2 was demonstrated to be the only protein kinase that phosphorylates RsfB in . Phosphorylation of Ser-63 inactivates RsfB to render it unable to interact with RsbW1. Our comparative RNA sequencing analysis of the wild-type strain of and its isogenic Δ mutant strain lacking the cytochrome oxidase of the respiratory electron transport chain revealed that expression of the SigF regulon is strongly induced under respiration-inhibitory conditions in an RsfB-dependent way.

Keywords

Mycobacterium SigF aa3 cytochrome c oxidase anti-anti-sigma factor anti-sigma factor electron transport chain partner switching system protein kinase

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