Format

Send to

Choose Destination
Biochem Biophys Res Commun. 2019 May 28;513(2):374-379. doi: 10.1016/j.bbrc.2019.04.019. Epub 2019 Apr 6.

Crystal structure of a transcription factor, GerE (PaGerE), from spore-forming bacterium Paenisporosarcina sp. TG-14.

Author information

1
Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
2
Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, Republic of Korea.
3
Division of Life Sciences, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
4
College of Pharmacy and Research Institute of Pharmaceutical Sciences, Gyeongsang National University, Jinju, 52828, Republic of Korea.
5
College of Pharmacy, Chung-Ang University, 84 Heukseok-ro, Dongjak, Seoul, 06974, Republic of Korea.
6
Department of Chemistry, Pukyong National University, 45 Yongso-ro, Busan, 48513, Republic of Korea.
7
Unit of Polar Genomics, Korea Polar Research Institute, Incheon, 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, Republic of Korea. Electronic address: junhyucklee@kopri.re.kr.

Abstract

In cold and harsh environments such as glaciers and sediments in ice cores, microbes can survive by forming spores. Spores are composed of a thick coat protein, which protects against external factors such as heat-shock, high salinity, and nutrient deficiency. GerE is a key transcription factor involved in spore coat protein expression in the mother cell during sporulation. GerE regulates transcription during the late sporulation stage by directly binding to the promoter of cotB gene. Here, we report the crystal structure of PaGerE at 2.09 Å resolution from Paenisporosarcina sp. TG-14, which was isolated from the Taylor glacier. The PaGerE structure is composed of four α-helices and adopts a helix-turn-helix architecture with 68 amino acid residues. Based on our DNA binding analysis, the PaGerE binds to the promoter region of CotB to affect protein expression. Additionally, our structural comparison studies suggest that DNA binding by PaGerE causes a conformational change in the α4-helix region, which may strongly induce dimerization of PaGerE.

KEYWORDS:

GerE; Paenisporosarcina sp. TG-14; Spore; X-ray crystallography

PMID:
30967265
DOI:
10.1016/j.bbrc.2019.04.019
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center