CesA protein is included in the terminal complex of Acetobacter

• Sun, Shi-jing

  Research Institute for Sustainable Humanosphere (RISH)Kyoto University

• Imai, Tomoya

  Research Institute for Sustainable Humanosphere (RISH)Kyoto University

• Sugiyama, Junji

  Research Institute for Sustainable Humanosphere (RISH)Kyoto University

• Kimura, Satoshi

  Research Institute for Sustainable Humanosphere (RISH)Kyoto University・Graduate School of Agricultural and Life ScienceThe University of Tokyo

Abstract

Cellulose is a major biopolymer on the earth that is produced by cellulose synthase in the cell membrane of living organisms. Cellulose synthase is a hetero-subunit complex composed of several different protein subunits, and is visualized as a supermolecular complex called a “terminal complex” by electron microscopy. Such supermolecular organization of an enzyme complex is believed to be important for the fiber formation or crystallization of cellulose microfibrils in cellulose biosynthesis. In the case of the cellulose-producing bacterium Acetobacter, it is hypothesized that the enzyme complex includes at least six subunits given its genetic constitution. However, to date, only three of these molecules have been experimentally confirmed as the subunits included in the terminal complex: CesB, CesD, and ccp2. In this study, we used fluorescence immuno-microscopy to show that CesA protein, the catalytic subunit, is included in the terminal complex of Acetobacter. Furthermore we discuss the obtained microscopic data for improving our understanding of the molecular organization of the bacterial cellulose synthase complex.

Journal

• Cellulose

  Cellulose 24 (5), 2017-2027, 2017-05

  Springer Nature

Keywords

• CesA
• Cellulose synthase complex
• Terminal complex
• Immunolabeling

Details

• CRID: 1050282810834211584
• NII Article ID: 120006463748
• ISSN: 09690239
• ISSN: 1572882X
• DOI: 10.1007/s10570-017-1237-6
• HANDLE: 2433/230960
• Web Site: http://link.springer.com/content/pdf/10.1007/s10570-017-1237-6.pdf
• Web Site: http://link.springer.com/article/10.1007/s10570-017-1237-6/fulltext.html
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • Crossref
  • CiNii Articles
  • KAKEN