Escherichia coli -: A model system that benefits from and contributes to the evolution of proteomics

被引:44
作者
Lee, PS [1 ]
Lee, KH [1 ]
机构
[1] Cornell Univ, Sch Chem & Biomol Engn, Ithaca, NY 14853 USA
关键词
proteomics; 2DE map; MALDI-TOFTOF;
D O I
10.1002/bit.10848
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
The large body of knowledge about Escherichia coli makes it a useful model organism for the expression of heterologous proteins. Proteomic studies have helped to elucidate the complex cellular responses of E. coli and facilitated its use in a variety of biotechnology applications. Knowledge of basic cellular processes provides the means for better control of heterologous protein expression. Beyond such important applications, E. coli is an ideal organism for testing new analytical technologies because of the extensive knowledge base available about the organism. For example, improved technology for characterization of unknown proteins using mass spectrometry has made two-dimensional electrophoresis (2DE) studies more useful and more rewarding, and much of the initial testing of novel protocols is based on well-studied samples derived from E. coli. These techniques have facilitated the construction of more accurate 2DE maps. In this review, we present work that led to the 2DE databases, including a new map based on tandem time-of-flight (TOF) mass spectrometry (MS); describe cellular responses relevant to biotechnology applications; and discuss some emerging proteomic techniques. (C) 2003 Wiley Periodicals, Inc.
引用
收藏
页码:801 / 814
页数:14
相关论文
共 134 条
  • [121] 2-N
  • [122] Walker AK, 2001, ELECTROPHORESIS, V22, P933, DOI 10.1002/1522-2683()22:5<933::AID-ELPS933>3.0.CO
  • [123] 2-9
  • [124] Quantitative proteomics strategy involving the selection of peptides containing both cysteine and histidine from tryptic digests of cell lysates
    Wang, SH
    Zhang, X
    Regnier, FE
    [J]. JOURNAL OF CHROMATOGRAPHY A, 2002, 949 (1-2) : 153 - 162
  • [125] Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli
    Weichart, D
    Querfurth, N
    Dreger, M
    Hengge-Aronis, R
    [J]. JOURNAL OF BACTERIOLOGY, 2003, 185 (01) : 115 - 125
  • [126] Weinberger SR, 2002, ELECTROPHORESIS, V23, P3182, DOI 10.1002/1522-2683(200209)23:18<3182::AID-ELPS3182>3.0.CO
  • [127] 2-5
  • [128] Short- and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose-limited growth conditions in continuous culture and vice versa
    Wick, LM
    Quadroni, M
    Egli, T
    [J]. ENVIRONMENTAL MICROBIOLOGY, 2001, 3 (09) : 588 - 599
  • [129] From proteins to proteomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis
    Wilkins, MR
    Pasquali, C
    Appel, RD
    Ou, K
    Golaz, O
    Sanchez, JC
    Yan, JX
    Gooley, AA
    Hughes, G
    HumpherySmith, I
    Williams, KL
    Hochstrasser, DF
    [J]. BIO-TECHNOLOGY, 1996, 14 (01): : 61 - 65
  • [130] Protein identification with N and C-terminal sequence tags in proteome projects
    Wilkins, MR
    Gasteiger, E
    Tonella, L
    Ou, K
    Tyler, M
    Sanchez, JC
    Gooley, AA
    Walsh, BJ
    Bairoch, A
    Appel, RD
    Williams, KL
    Hochstrasser, DF
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1998, 278 (03) : 599 - 608