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Microbiology 155 (2009), 741-750; DOI  10.1099/mic.0.024075-0
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Microbiology 155 (2009), 741-750; DOI  10.1099/mic.0.024075-0
© 2009 Society for General Microbiology

Scanning the Corynebacterium glutamicum R genome for high-efficiency secretion signal sequences

Keiro Watanabe1, Yoshiki Tsuchida1,2, Naoko Okibe1, Haruhiko Teramoto1, Nobuaki Suzuki1, Masayuki Inui1 and Hideaki Yukawa1

1 Molecular Microbiology and Biotechnology Group, Research Institute of Innovative Technology for the Earth (RITE), 9-2, Kizugawadai, Kizugawa, Kyoto 619-0292, Japan
2 Honda R&D Co., Ltd, 1-4-1 Chuo Wako, Saitama 351-0193, Japan

Correspondence
Hideaki Yukawa
mmg-lab{at}rite.or.jp

Systematic screening of secretion proteins using an approach based on the completely sequenced genome of Corynebacterium glutamicum R revealed 405 candidate signal peptides, 108 of which were able to heterologously secrete an active-form {alpha}-amylase derived from Geobacillus stearothermophilus. These comprised 90 general secretory (Sec)-type, 10 twin-arginine translocator (Tat)-type and eight Sec-type with presumptive lipobox peptides. Only Sec- and Tat-type signals directed high-efficiency secretion. In two assays, 11 of these signals resulted in 50- to 150-fold increased amounts of secreted {alpha}-amylase compared with the well-known corynebacterial secretory protein PS2. While the presence of an AXA motif at the cleavage sites was readily apparent, it was the presence of a glutamine residue adjacent to the cleavage site that may affect secretion efficiency.

Abbreviations: Sec, general secretory; SPase, signal peptidase; Tat, twin-arginine translocator

Two supplementary tables, listing oligonucleotide DNA primers used in this study and putative secretory proteins examined in this work, are available with the online version of this paper.






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