Characterization of the Erwinia carotovora pelB gene and its product pectate lyase
Open accessAbstract
The pelB gene encodes pectate lyase B, one of three pectate lyases identified in Erwinia carotovora EC. Pectate lyase B was purified from Escherichia coli containing the pelB gene on a recombinant plasmid. The activity of the protein was optimal at a pH of 8.3. The amino acid composition, N-terminal amino acid sequence, and C-terminal peptide sequence were determined and compared with the polypeptide sequence deduced from the DNA sequence of pelB. Purified pectate lyase B started at amino acid 23 of the predicted sequence, suggesting that a 22-amino-acid leader peptide had been removed. Pectate lyase B of E. carotovora EC and pectate lyase B of E. chrysanthemi EC16 contain 352 and 353 amino acids, respectively (N. T. Keen, S. Tanaki, W. Belser, D. Dahlbeck, and B. Staskawicz, J. Bacteriol. 168:595-606, 1986). The two proteins are 72% homologous on the basis of DNA sequence data, and 75% of the amino acids are identical.
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The 22 amino acids long PelB signal sequence from Erwinia carotovora is the most frequently used for transportation of Fabs and scFvs.
“The 22 amino acids long PelB (pectate lyase B) signal sequence from Erwinia carotovora [157] is the most frequently used for transportation of the Fabs [88,96] and scFvs [30,101,158,159].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [157]
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araB Gene and nucleotide sequence of the araC gene of Erwinia carotovora
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Zheng, J. H., Nguyen, V. H., Jiang, S.-N., Park, S.-H., Tan, W., Hong, S. H., Shin, M. G., Chung, I.-J., Hong, Y., Bom, H.-S., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aak9537 · Cited by 588 · see citing works
Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
Construction and periplasmic expression of the Anti-EGFRvIII ScFv antibody gene in Escherichia coli
DEWI, K. S. (2016) · Scientia Pharmaceutica · doi:10.3797/scipharm.isp.2015.06 · Cited by 18 · see citing works
- Authors
- Lei, S. P., Lin, H. C., Wang, S. S., Callaway, J., & Wilcox, G.
- Affiliations
- University of California, Los Angeles (US)
- ORCID
- Wang, S S
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1987-09
- Volume
- 169
- Issue
- 9
- Pages
- 4379-4383
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC213756
- OpenAlex
- W1891302139
- Cited by
- 285
- References
- 8
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 8 · 2023: 4 · 2022: 10 · 2021: 10 · 2020: 5 · 2019: 6 · 2018: 8 · 2017: 6 · 2016: 14 · 2015: 9 · 2014: 8 · 2013: 4 · 2012: 10
- FWCI
- 8.36
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM30491)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Pathogenic Bacteria Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
- Keywords
- Erwinia carotovora, pectate lyase, recombinant protein expression, Escherichia coli, amino acid sequence, N-terminal sequence, C-terminal sequence, leader peptide, protein purification, pH optimum, Erwinia chrysanthemi, sequence homology
- MeSH terms
- Amino Acid Sequence, Amino Acids, Base Sequence, Cloning, Molecular, DNA Restriction Enzymes, DNA, Bacterial, Erwinia, Gene Expression Regulation, Genes, Bacterial, Peptide Fragments, Polysaccharide-Lyases, Promoter Regions, Genetic, Sequence Homology, Nucleic Acid
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