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 inBioscience, biotechnology, and biochemistry Vol. 72; no. 12; pp. 3158 - 3166
Main Authors Cheng, Y.(Laval Univ., Quebec (Canada)), Avis, T.J, Bolduc, S, Zhao, Y, Anguenot, R, Neveu, B, Labbe, C, Belzile, F, Belanger, R.R
Format Journal Article
LanguageEnglish
Published Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.12.2008
Japan Society for Bioscience Biotechnology and Agrochemistry
Oxford University Press
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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.
Bibliography:2009000728
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ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.80340