Article Abstract:
The cell-wall-anchored cellulose (Avicel)-binding protein (AbpS) from Streptomyces reticuli has been studied using electron microscopy techniques. AbpS is a 35-kDa protein that interacts strongly with crystalline but not with soluble types of cellulose. Polymerase chain reactions were used in amplifying the complete abpS genes or the truncated abpS genes that were shortened at the 5' end. Results indicated that the NH2 terminus of AbpS protrudes from the murein layer of S. reticuli. An examination of the ultrathin sections of the cell wall showed that AbpS is tightly and covalently linked to the polyglucane layer.
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Article Abstract:
The fusH gene which encodes the Streptomyces lividans FusH extracellular enzyme was cloned and sequenced by utilizing a deduced oligonucleotide probe. Analysis of the clone fusH gene from Streptomyces lividans subgenomic DNA library indicated the presence of two putative start codons with three directly repeated sequences. Furthermore, biochemical analysis of the FusH esterase indicated the presence of a GDS motif that was similar to other microbial esterases.
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Article Abstract:
The 4.3 kb amplifiable DNA unit (AUD) was characterized in the wild-type Streptomyces lividans 66 genome. Its sequence was compared with the corresponding amplified DNA sequence (ADS). A novel 23kDa protein encoded by the AUD and ADS was identified and shown to be associated with the substrate hyphae of the wild-type and the ADS-containing variant. Microscopic examination revealed that the strain carrying the ADS formed hyphal bulges apical vesicles.
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