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Applied and Environmental Microbiology, May 2006, p. 3797-3801, Vol. 72, No. 5
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.5.3797-3801.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Improvement of an Unusual Twin-Arginine Transporter Leader Peptide by a Codon-Based Randomization Approach{dagger}

Olga Monroy-Lagos, Xavier Soberon, Paul Gaytan, and Joel Osuna*

Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología/ Universidad Nacional Autónoma de México, Cuernavaca, México

Received 13 September 2005/ Accepted 2 March 2006

Secretion of Escherichia coli penicillin acylase was improved by codon-based random mutagenesis of its signal peptide. The mutagenesis technology was applied to the gene region coding for positions Lys2 to Thr13 (N half) and Ala14 to Leu25 (C half) of the signal peptide. Protein secretion was higher in several signal peptide variants (up to fourfold with respect to the wild-type value).

* Corresponding author. Mailing address: Instituto de Biotecnología/UNAM, Av. Universidad 2001, Col. Chamilpa, 62210 Cuernavaca, Morelos, México. Phone: (52) (777) 329 1605. Fax: (52) (777) 317 2388. E-mail: joel{at}ibt.unam.mx.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

Applied and Environmental Microbiology, May 2006, p. 3797-3801, Vol. 72, No. 5
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.5.3797-3801.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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