Our objective is to biochemically and structurally characterize the proteins involved in cellulose synthesis. Gluconacetobacter hansenii, a Gram negative bacterium capable of secreting copious amounts of cellulose, is our model organism. We have sequenced the genome of G. hansenii 23769, in an attempt to unravel the proteomic networks leading to cellulose synthesis. Our work has also contributed to determination of the solution structure and localization of a protein (AcsD), known to play a role in the crystallinity of bacterial cellulose. In addition to this, we have shown for the first time that the cellulose synthase protein (AcsAB), though encoded by a single gene, is processed in the cells to form to polypeptide cleavage products. Work is ongoing to elucidate the exact site of cleavage using mass spectrometry and N-terminal sequencing. We have also purified the cellulose synthase activity using a native in-gel zymogram method and are thus, a step closer to identifying the catalytic core complex of proteins involved in cellulose synthesis, using mass-spectrometric techniques. Solubilization of the heterologously expressed bacterial cellulose synthase substrate binding region, has provided us a protein for crystallographic studies. Thus, my work has enabled us to explore bacterial cellulose synthesis from several different perspectives.

Biochemistry of bacterial cellulose synthesis: How do bacteria spin the yarn?

243rd National Meeting (2012)

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