On the functionality of the N-terminal domain in xylanase 10A from Ruminococcus albus 8
Autor: | Alberto A. Iglesias, Alem Storani, Sergio Adrian Guerrero |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0106 biological sciences
0301 basic medicine Mutant Bioengineering ATP-binding cassette transporter 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Dithiothreitol Substrate Specificity law.invention Cell membrane purl.org/becyt/ford/1 [https] 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Cellulase Polysaccharides law 010608 biotechnology Ruminococcus medicine purl.org/becyt/ford/1.6 [https] chemistry.chemical_classification Xylanase Recombinant Proteins 030104 developmental biology Enzyme medicine.anatomical_structure chemistry Recombinant DNA Xylans Carbohydrate-binding module Biotechnology |
Zdroj: | CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET |
Popis: | We analyzed the structure to function relationships in Ruminococcus albus 8 xylanase 10A (RalXyn10A) finding that the N-terminus 34-amino acids sequence (N34) in the protein is particularly functional. We performed the recombinant wild type enzyme’s characterization and that of the truncated mutant lacking the N34 extreme (RalΔN34Xyn10A). The truncated enzyme exhibited about half of the activity and reduced affinity for binding to insoluble saccharides. These suggest a (CBM)-like function for the N34 motif. Besides, RalXyn10A activity was diminished by redox agent dithiothreitol, a characteristic absent in RalΔN34Xyn10A. The N34 sequence exhibited a significant similarity with protein components of the ABC transporter of the bacterial membrane, and this motif is present in other proteins of R. albus 8. Data suggest that N34 would confer RalXyn10A the capacity to interact with polysaccharides and components of the cell membrane, enhancing the degradation of the substrate and uptake of the products by the bacterium. Fil: Storani, Alem. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina |
Databáze: | OpenAIRE |
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