Abstract
The secretory efficiency of recombinant xylanase xynB from yeast Pichia pastoris between the alpha-factor preprosequence and a classical mammalian signal peptide derived from bovine beta-casein was compared. The results showed that although the bovine beta-casein signal peptide could direct highlevel secretion of recombinant xylanase, it was relatively less efficient than the alpha-factor preprosequence. In contrast, the bovine beta-casein signal peptide caused remarkably more recombinant xylanase trapped intracellularly. Realtime RT-PCR analysis indicated that the difference in the secretory level between the two signal sequences was not due to the difference in the transcriptional efficiency.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Caseins / chemistry
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Caseins / genetics*
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Cattle
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Endo-1,4-beta Xylanases / chemistry
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Endo-1,4-beta Xylanases / genetics
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Endo-1,4-beta Xylanases / metabolism*
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Gene Expression
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Mating Factor
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / genetics*
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Pichia / genetics*
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Pichia / metabolism
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Protein Engineering*
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Protein Sorting Signals*
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Protein Transport
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Streptomyces / enzymology*
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beta-Glucosidase / chemistry
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beta-Glucosidase / genetics
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beta-Glucosidase / metabolism*
Substances
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Bacterial Proteins
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Caseins
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Peptides
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Protein Sorting Signals
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Recombinant Fusion Proteins
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Mating Factor
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beta-Glucosidase
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Endo-1,4-beta Xylanases
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XynB xylanase