Rapid translation system: A novel cell-free way from gene to protein

Hoffmann, Michael; Nemetz, Cordula; Madin, Kairat; Buchberger, Bernd

doi:10.1016/s1387-2656(04)10001-x

Cited by 24 publications

(18 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Most of these lectins are not expressed in normal tissues but their expression is induced after welldefined stress conditions, such as salt stress, drought, or plant hormone treatment (Van Damme et al 2003, 2004. Nictaba is a lectin produced in the tobacco plant (Nicotiana tabacum cv Samsun NN) after exposure to the plant hormone jasmonic acid methyl ester (Chen et al 2002) as well as after insect herbivory by caterpillars (Lannoo et al 2007).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cell-free expression and functionality analysis of the tobacco lectin

Vandenborre

Lannoo

Smagghe

et al. 2008

In Vitro Cell.Dev.Biol.-Animal

View full text Add to dashboard Cite

The Nicotiana tabacum lectin, called Nictaba, is a nucleocytoplasmic plant lectin expressed in tobacco leaves after exogenous application of specific jasmonates and upon insect herbivory. Since the lectin concentrations are rather low, huge amounts of plant material are needed to purify milligram quantities of the protein. In addition, the purified lectin fractions are always contaminated with low molecular weight compounds such as phenols. In an attempt to improve and facilitate the purification of the tobacco lectin in reasonable amounts, an in vitro-coupled transcription/translation system based on an Escherichia coli lysate was used to express the lectin gene. Recombinant expression levels could be enhanced by an adapted codon usage. Recombinant lectin was purified, biochemically characterized and found to be biologically active. The biological activity of the recombinant lectin towards insect epithelial midgut cells was clearly demonstrated in a functional bio-assay and the internal cellular localization was analyzed using immunocytochemical techniques.

show abstract

Section: Introductionmentioning

confidence: 99%

“…as much as 400 µg/ml recombinant protein in a 2-h batch reaction. An advantage of the system is the ability to scaleup to a continuous exchange cell-free format (CECF) to allow protein expression up to milligrams of protein production in 24 h (Betton 2003;Hoffmann et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Cell-free expression and functionality analysis of the tobacco lectin

Vandenborre

Lannoo

Smagghe

et al. 2008

In Vitro Cell.Dev.Biol.-Animal

View full text Add to dashboard Cite

show abstract

“…cell adhesion [64], innate immunity [3], CO 2 assimilation in metabolic pathways [30], extracellular matrix degradation [2] and membrane construction [17,44,85]) as well as the binding properties of retrocyclins [14], apotosis regulators [42], antimicrobial peptides [23], glycosphingolipids [97], barley -amylase/subtilisin inhibitor [66], amelogenin [67], lysenin [45], lectins [65], endoxylases [40], connexins [21], selectins [25], phosphoinositides [71], carbohydrates [20,70,72], HIV proteins [48,91], tumor necrosis factor receptor superfamily [95] and the insulin-like growth factor system [58]. Other reviews highlight the integration of optical biosensors with complementary technologies in areas of applied research, including drug development and chemical genetics [1,50,73,83,88], plant proteomics [33], gene and protein expression [29,35,86], antibody optimization [5,46,62], food industry [4,47,54,61,79], bioprocessing and manufacturing [12,…”

Section: Reviews Theory and Methodsmentioning

confidence: 99%

Survey of the year 2004 commercial optical biosensor literature

Rich

Myszka

2005

J of Molecular Recognition

115

View full text Add to dashboard Cite

The year 2004 represents a milestone for the biosensor research community: in this year, over 1000 articles were published describing experiments performed using commercially available systems. The 1038 papers we found represent a $ 10% increase over the past year and demonstrate that the implementation of biosensors continues to expand at a healthy pace. We evaluated the data presented in each paper and compiled a 'top 10' list. These 10 articles, which we recommend every biosensor user reads, describe wellperformed kinetic, equilibrium and qualitative/screening studies, provide comparisons between binding parameters obtained from different biosensor users, as well as from biosensor-and solution-based interaction analyses, and summarize the cutting-edge applications of the technology. We also re-iterate some of the experimental pitfalls that lead to sub-optimal data and over-interpreted results. We are hopeful that the biosensor community, by applying the hints we outline, will obtain data on a par with that presented in the 10 spotlighted articles. This will ensure that the scientific community at large can be confident in the data we report from optical biosensors.

show abstract

“…Cell-free protein production is achieved by combining a crude lysate from growing cells, which contains all the necessary enzymes and machinery for protein synthesis (including transcription and translation), with the exogenous supply of essential amino acids, nucleotides, salts, and energy-generating factors and introducing exogenous messages including RNA (mRNA) or DNA as template into the system [7,8]. The cell-free system presents two obvious advantages over in vivo protein expression.…”

Section: Introductionmentioning

confidence: 99%

Progress in Chemical Synthesis of Peptides and Proteins

Hou

Zhang

Liu

2017

Trans. Tianjin Univ.

View full text Add to dashboard Cite

For the proteins that cannot be expressed exactly by cell expression technology (e.g., proteins with multiple posttranslational modifications or toxic proteins), chemical synthesis is an important substitute. Given the limited peptide length offered by solid-phase peptide synthesis invented by Professor Merrifield, peptide ligation plays a key role in long peptide or protein synthesis by ligating two small peptides to a long one. Moreover, high-molecularweight proteins must be synthesized using two or more peptide ligation steps, and sequential peptide ligation is such an efficient way. In this paper, we reviewed the development of chemical protein synthesis, including solid-phase peptide synthesis, chemical ligation, and sequential chemical ligation.

show abstract

Rapid translation system: A novel cell-free way from gene to protein

Cited by 24 publications

References 19 publications

Cell-free expression and functionality analysis of the tobacco lectin

Cell-free expression and functionality analysis of the tobacco lectin

Survey of the year 2004 commercial optical biosensor literature

Progress in Chemical Synthesis of Peptides and Proteins

Contact Info

Product

Resources

About