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

Keiro Watanabe, Yoshiki Tsuchida, Naoko Okibe, Haruhiko Teramoto, Nobuaki Suzuki, Masayuki Inui, Hideaki Yukawa

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

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 α-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 Secand Tat-type signals directed high-efficiency secretion. In two assays, 11 of these signals resulted in 50- to 150-fold increased amounts of secreted α-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.

Original languageEnglish
Pages (from-to)741-750
Number of pages10
JournalMicrobiology
Volume155
Issue number3
DOIs
Publication statusPublished - 2009

All Science Journal Classification (ASJC) codes

  • Microbiology

Fingerprint Dive into the research topics of 'Scanning the Corynebacterium glutamicum R genome for high-efficiency secretion signal sequences'. Together they form a unique fingerprint.

Cite this