Post-translational processing of modular xylanases from Streptomyces is dependent on the carbohydrate-binding module

• Published in: Journal of industrial microbiology & biotechnology 2011-09, Vol.38 (9), p.1419-1426
• Main Authors: Díaz, Margarita, Fernández-Ábalos, José M., Soliveri, Juan, Copa-Patiño, José L., Santamaría, Ramón I.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Biochemistry; Bioinformatics; Biological and medical sciences; Biomedical and Life Sciences; Biotechnology; Carbohydrates; Catalysis; Catalytic Domain; Cellulose; Cellulose - metabolism; Cloning; E coli; Enzymes; Ethanol; Fundamental and applied biological sciences. Psychology; Genes; Genetic Engineering; Inorganic Chemistry; Laboratories; Life Sciences; Microbiology; Molecular Sequence Data; Original Paper; Protein folding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Proteins; Recombinant Fusion Proteins - metabolism; Streptomyces; Streptomyces - enzymology; Streptomyces avermitilis; Streptomyces halstedii; Studies; Xylans - metabolism; Xylosidases - chemistry; Xylosidases - genetics; Xylosidases - metabolism
• ISSN: 1367-5435; 1476-5535
• DOI: 10.1007/s10295-010-0927-y

Xylanases are very often modular enzymes composed of one or more catalytic domains and carbohydrate-binding modules (CBMs) connected by a flexible linker region. Usually, when these proteins are processed they lose their carbohydrate-binding capacity. Here, the role of the linker regions and cellulose- or xylan-binding domains in the processing of Xys1L from Streptomyces halstedii JM8 and Xyl30L from Streptomyces avermitilis UAH30 was studied. Xys1 variants with different linker lengths were tested, these being unable to avoid protein processing. Moreover, several fusion proteins between the Xys1 and Xyl30 domains were obtained and their proteolytic stability was studied. We demonstrate that CBM processing takes place even in the complete absence of the linker sequence. We also show that the specific carbohydrate module determines this cleavage in the proteins studied.