Missense mutations in a transmembrane domain of the Komagataeibacter xylinus BcsA lead to changes in cellulose synthesis
| Autor: | Silvia Blank, Dario Bonetta, Reza Alipour Moghadam Esfahani, Luis Salgado, Janice L. Strap |
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| Rok vydání: | 2019 |
| Předmět: |
Microbiology (medical)
Komagataeibacter xylinus Mutant lcsh:QR1-502 Mutation Missense 02 engineering and technology Biology Microbiology lcsh:Microbiology Pellicin 03 medical and health sciences chemistry.chemical_compound Chalcones Bacterial Proteins Protein Domains Drug Resistance Bacterial Missense mutation Cellulose Crystallinity 030304 developmental biology Glucan chemistry.chemical_classification 0303 health sciences Gluconacetobacter xylinus Oxocins Mutagenesis BcsA 021001 nanoscience & nanotechnology Forward genetics Transmembrane domain chemistry Biochemistry Glucosyltransferases Crystallization 0210 nano-technology Research Article |
| Zdroj: | BMC Microbiology BMC Microbiology, Vol 19, Iss 1, Pp 1-13 (2019) |
| DOI: | 10.21203/rs.2.9716/v1 |
| Popis: | Background Cellulose is synthesized by an array of bacterial species. Komagataeibacter xylinus is the best characterized as it produces copious amounts of the polymer extracellularly. Despite many advances in the past decade, the mechanisms underlying cellulose biosynthesis are not completely understood. Elucidation of these mechanisms is essential for efficient cellulose production in industrial applications. Results In an effort to gain a better understanding of cellulose biosynthesis and its regulation, cellulose crystallization was investigated in K. xylinus mutants resistant to an inhibitor of cellulose I formation, pellicin. Through the use of forward genetics and site-directed mutagenesis, A449T and A449V mutations in the K. xylinus BcsA protein were found to be important for conferring high levels of pellicin resistance. Phenotypic analysis of the bcsAA449T and bcsAA449V cultures revealed that the mutations affect cellulose synthesis rates and that cellulose crystallinity is affected in wet pellicles but not dry ones. Conclusions A449 is located in a predicted transmembrane domain of the BcsA protein suggesting that the structure of the transmembrane domain influences cellulose crystallization either by affecting the translocation of the nascent glucan chain or by allosterically altering protein-protein interactions. |
| Databáze: | OpenAIRE |
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