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Isolation and heterologous expressi
Isolation and heterologous expression of GalOx-encoding gene
Mycelium of F. sambucinum from a culture grown in liquid medium was harvested and the genomic DNA was isolated. Degenerated primers based on published sequences were used to amplify the gao gene coding for GalOx including its signal sequence. The gene consists of an open reading frame of 2037 bp encoding a polypeptide of 679 amino acids. The sequence (GenBank accession No. KM052576) contains no introns and a 37 amino acid prepro sequence. The similarity to the protein sequences of GalOx from F. graminearum [5] and F. oxysporum [68] are 96% and 81%, respectively. The amino acid sequence derived from the F. sambucinum gao gene was used to generate a three-dimensional homology model based on the published structure of mature GalOx (1gog) from F. graminearum [5] using SWISS-MODEL [61], [62] and [63] ( Fig. 1). The amino acids in the active site ( Fig. 1B) as well as in the second shell surrounding it are completely conserved. The architecture of the substrate-binding pocket as well as the residues responsible for copper binding are also identical. The changes in amino acid sequences are mainly found on the surface of the protein.
Mycelium of F. sambucinum from a culture grown in liquid medium was harvested and the genomic DNA was isolated. Degenerated primers based on published sequences were used to amplify the gao gene coding for GalOx including its signal sequence. The gene consists of an open reading frame of 2037 bp encoding a polypeptide of 679 amino acids. The sequence (GenBank accession No. KM052576) contains no introns and a 37 amino acid prepro sequence. The similarity to the protein sequences of GalOx from F. graminearum [5] and F. oxysporum [68] are 96% and 81%, respectively. The amino acid sequence derived from the F. sambucinum gao gene was used to generate a three-dimensional homology model based on the published structure of mature GalOx (1gog) from F. graminearum [5] using SWISS-MODEL [61], [62] and [63] ( Fig. 1). The amino acids in the active site ( Fig. 1B) as well as in the second shell surrounding it are completely conserved. The architecture of the substrate-binding pocket as well as the residues responsible for copper binding are also identical. The changes in amino acid sequences are mainly found on the surface of the protein.
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Cô lập và heterologous biểu hiện của gen mã hóa GalOxKhuẩn ty thể của F. sambucinum từ một nền văn hóa phát triển trong môi trường lỏng được thu hoạch và DNA gen đã bị cô lập. Nhâ chất mồi dựa trên trình tự xuất bản được sử dụng để khuyếch đại cao gen mã hóa cho GalOx bao gồm chuỗi tín hiệu. Gen bao gồm một khung đọc mở của 2037 bp mã hóa một polypeptide 679 axit amin. Trình tự (gia nhập GenBank số KM052576) có chứa không có introns và một acid amin 37 prepro tự. Sự tương tự với chuỗi protein của GalOx từ F. graminearum [5] và F. oxysporum [68] là 96% và 81%, tương ứng. Trình tự axit amin bắt nguồn từ F. sambucinum gao gen đã được sử dụng để tạo ra một mô hình ba chiều homology dựa trên cấu trúc được công bố của trưởng thành GalOx (1gog) từ F. graminearum [5] bằng cách sử dụng SWISS-mô hình [61], [62] và [63] (hình 1). Các axit amin trong trang web đang hoạt động (hình 1B) cũng như trong quả đạn pháo thứ hai xung quanh nó hoàn toàn được bảo tồn. Kiến trúc của túi bề mặt-ràng buộc và dư lượng chịu trách nhiệm cho đồng ràng buộc cũng là giống hệt nhau. Những thay đổi trong trình tự axit amin chủ yếu được tìm thấy trên bề mặt của protein.
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Isolation and heterologous expression of GalOx-encoding gene
Mycelium of F. sambucinum from a culture grown in liquid medium was harvested and the genomic DNA was isolated. Degenerated primers based on published sequences were used to amplify the gao gene coding for GalOx including its signal sequence. The gene consists of an open reading frame of 2037 bp encoding a polypeptide of 679 amino acids. The sequence (GenBank accession No. KM052576) contains no introns and a 37 amino acid prepro sequence. The similarity to the protein sequences of GalOx from F. graminearum [5] and F. oxysporum [68] are 96% and 81%, respectively. The amino acid sequence derived from the F. sambucinum gao gene was used to generate a three-dimensional homology model based on the published structure of mature GalOx (1gog) from F. graminearum [5] using SWISS-MODEL [61], [62] and [63] ( Fig. 1). The amino acids in the active site ( Fig. 1B) as well as in the second shell surrounding it are completely conserved. The architecture of the substrate-binding pocket as well as the residues responsible for copper binding are also identical. The changes in amino acid sequences are mainly found on the surface of the protein.
Mycelium of F. sambucinum from a culture grown in liquid medium was harvested and the genomic DNA was isolated. Degenerated primers based on published sequences were used to amplify the gao gene coding for GalOx including its signal sequence. The gene consists of an open reading frame of 2037 bp encoding a polypeptide of 679 amino acids. The sequence (GenBank accession No. KM052576) contains no introns and a 37 amino acid prepro sequence. The similarity to the protein sequences of GalOx from F. graminearum [5] and F. oxysporum [68] are 96% and 81%, respectively. The amino acid sequence derived from the F. sambucinum gao gene was used to generate a three-dimensional homology model based on the published structure of mature GalOx (1gog) from F. graminearum [5] using SWISS-MODEL [61], [62] and [63] ( Fig. 1). The amino acids in the active site ( Fig. 1B) as well as in the second shell surrounding it are completely conserved. The architecture of the substrate-binding pocket as well as the residues responsible for copper binding are also identical. The changes in amino acid sequences are mainly found on the surface of the protein.
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