4.4 Article

Crystal structures of Streptomyces tsukubaensis sigma factor SigG1 and anti-sigma RsfG

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JOURNAL OF STRUCTURAL BIOLOGY
卷 215, 期 4, 页码 -

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ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2023.108038

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a/anti-a pair; Streptomyces tsukubaensis; Crystal structures; ECF56

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Transcription of specific genes in bacteria under environmental stress is initiated by extracytoplasmic function (ECF) α factors. The crystal structures of Streptomyces tsukubaensis SigG1 and anti-sigma RsfG were determined, revealing their compact conformations and metal binding motifs. These structures provide insights into the involvement of the ECF56 SigG1-RsfG system in metal-ion homeostasis.
Transcription of specific genes in bacteria under environmental stress is frequently initiated by extracytoplasmic function (ECF) a factors. ECFs a factors harbour two conserved domains, a2 and a4, for transcription initiation by recognition of the promoter region and recruitment of RNA polymerase (RNAP). The crystal structure of Strep-tomyces tsukubaensis SigG1, an ECF56-family a factor, was determined revealing a2, a4 and the additional carboxi-terminal domain SnoaL_2 tightly packed in a compact conformation. The structure of anti-sigma RsfG was also determined by X-ray crystallography and shows a rare B-barrel fold. Analysis of the metal binding motifs inside the protein barrel are consistent with Fe(III) binding, which is in agreement with previous findings that the Streptomyces tsukubaensis ECF56 SigG1-RsfG system is involved in metal-ion homeostasis.

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