Electron Microscopy Studies of Cell-Wall-Anchored Cellulose (Avicel)-Binding Protein (AbpS) from Streptomyces reticuli

AUTOR(ES)

Walter, Stefan

FONTE

American Society for Microbiology

RESUMO

Streptomyces reticuli produces a 35-kDa cellulose (Avicel)-binding protein (AbpS) which interacts strongly with crystalline cellulose but not with soluble types of cellulose. Antibodies that were highly specific for the NH2-terminal part of AbpS were isolated by using truncated AbpS proteins that differed in the length of the NH2 terminus. Using these antibodies for immunolabelling and investigations in which fluorescence, transmission electron, or immunofield scanning electron microscopy was used showed that the NH2 terminus of AbpS protrudes from the murein layer of S. reticuli. Additionally, inspection of ultrathin sections of the cell wall, as well as biochemical experiments performed with isolated murein, revealed that AbpS is tightly and very likely covalently linked to the polyglucane layer. As AbpS has also been found to be associated with protoplasts, we predicted that a COOH-terminal stretch consisting of 17 hydrophobic amino acids anchors the protein to the membrane. Different amounts of AbpS homologues of several Streptomyces strains were synthesized.

Documentos Relacionados

• The Cell Wall-Anchored Streptomyces reticuli Avicel-Binding Protein (AbpS) and Its Gene
• Characterization of the Binding Protein-Dependent Cellobiose and Cellotriose Transport System of the Cellulose Degrader Streptomyces reticuli
• Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli
• Electron Microscopy of Staphylococcus aureus Cell Wall Lysis
• Electron Microscopy of the Cell Wall of Rickettsia prowazeki