Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains

被引:10
|
作者
Han, Mee-Jung [1 ]
Kim, Jin Young [2 ]
Kim, Jung A. [2 ]
机构
[1] Dongyang Univ, Dept Biomol & Chem Engn, Yeongju 750711, Gyeongbuk, South Korea
[2] Korea Basic Sci Inst, Mass Spectrometry Res Ctr, Cheongwon Gun 863883, Chungbuk, South Korea
基金
新加坡国家研究基金会;
关键词
Periplasmic proteins; Secretion; Escherichia coli; Proteome; Periplasmic fractionation; GENOME SEQUENCES; STRUCTURAL GENE; OSMOTIC SHOCK; PROTEIN; EXPRESSION; CLONING; ACID; LOCALIZATION; PURIFICATION; PHOSPHATASE;
D O I
10.1016/j.jbiosc.2013.09.008
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Escherichia coli typically secretes many proteins into the periplasmic space, and the periplasmic proteins have been used for the secretory production of various proteins by the biotechnology industry. However, the identity of all of the E. coli periplasmic proteins remains unknown. Here, high-resolution periplasmic proteome reference maps of the E. coli K-12 and B strains were constructed and compared. Of the 145 proteins identified by tandem mass spectrometry, 61 proteins were conserved in the two strains, whereas 11 and 12 strain-specific proteins were identified for the E. coli K-12 and B strains, respectively. In addition, 27 proteins exhibited differences in intensities greater than 2-fold between the K-12 and B strains. The periplasmic proteins MalE and OppA were the most abundant proteins in the two E. coli strains. Distinctive differences between the two strains included several proteins that were caused by genetic variations, such as CybC, FliC, FliY, KpsD, MgIB, ModA, and YbI119, hydrolytic enzymes, particularly phosphatases, glycosylases, and proteases, and many uncharacterized proteins. Compared to previous studies, the localization of many proteins, including 30 proteins for the K-12 strain and 53 proteins for the B strain, was newly identified as periplasmic. This study identifies the largest number of proteins in the E. coli periplasm as well as the dynamics of these proteins. Additionally, these findings are summarized as reference proteome maps that will be useful for studying protein secretion and may provide new strategies for the enhanced secretory production of recombinant proteins. (c) 2013, The Society for Biotechnology, Japan. All rights reserved.
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页码:437 / 442
页数:6
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