Recombinant protein secretion in Pseudozyma flocculosa and Pseudozyma antarctica with a novel signal peptide
Secretion of recombinant proteins aims to reproduce the correct posttranslational modifications of the expressed protein while simplifying its recovery. In this study, secretion signal sequences from an abundantly secreted 34-kDa protein (P34) from Pseudozyma flocculosa were cloned. The efficiency o...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 72; no. 12; pp. 3158 - 3166 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
Japan Society for Bioscience, Biotechnology, and Agrochemistry
01.12.2008
Japan Society for Bioscience Biotechnology and Agrochemistry Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | Secretion of recombinant proteins aims to reproduce the correct posttranslational modifications of the expressed protein while simplifying its recovery. In this study, secretion signal sequences from an abundantly secreted 34-kDa protein (P34) from Pseudozyma flocculosa were cloned. The efficiency of these sequences in the secretion of recombinant green fluorescent protein (GFP) was investigated in two Pseudozyma species and compared with other secretion signal sequences, from S. cerevisiae and Pseudozyma spp. The results indicate that various secretion signal sequences were functional and that the P34 signal peptide was the most effective secretion signal sequence in both P. flocculosa and P. antarctica. The cells correctly processed the secretion signal sequences, including P34 signal peptide, and mature GFP was recovered from the culture medium. This is the first report of functional secretion signal sequences in P. flocculosa. These sequences can be used to test the secretion of other recombinant proteins and for studying the secretion pathway in P. flocculosa and P. antarctica. |
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Bibliography: | 2009000728 F30 Q01 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.80340 |