A framework for designing transgenic crops - science, safety, and citizen’s concerns.

in Nature Biotechnology (2003), 21(11), 1274-1279

Forum Comment

in Science & Technology (2003), XX

Negotiating the precautionary principle: Regulatory and institutional roots of divergent US and EU positions

in International Journal of BioTechnology (2002), 4(1), 61-81

The precautionary principle has been a bone of contention in international negotiations on the governance of environmental and health risks. The US administration and European institutions often present ... [more ▼]

The precautionary principle has been a bone of contention in international negotiations on the governance of environmental and health risks. The US administration and European institutions often present opposing views on whether formal references to precaution help or hinder the global governance of risk, in particular where linked to world trade. The European Commission official position, backed by Council, Parliament and some Member States, advocates the principle's use in legal texts and pushes for the elaboration of international guidelines for its application. The proposed guidelines, whilst explicitly conforming to basic principles of trade law, include recommendations on broad socio-economic impact analyses of alternative risk mitigation measures and emphasise political aspects of decisions on risk. The US administration's official position papers oppose references to precaution and socio-economic impact analysis in international laws and guidelines on risk analysis. They mainly cite fears of abuse of the concept as guise for protectionist measures. In each administration a wide range of state and non-state actors with disparate views inform policy makers who then have to adopt one coherent position. This article suggests that overarching differences in the negotiating positions adopted by the US and European institutions, often attributed to culturally and politically rooted biases on risk and uncertainty, are also reflected in institutional practices and regulatory frameworks of the two jurisdictions. It recommends taking disparate institutional structures and regulatory frameworks into account in future deliberations on international guidelines on risk analysis. [less ▲]

Safety considerations of DNA in food

in Annals of Nutrition & Metabolism (2001), 45(6), 1-20

Recombinant DNA techniques are capable of introducing genetic changes into food organisms that are more predictable than those introduced through conventional breeding techniques. This review discusses ... [more ▼]

Recombinant DNA techniques are capable of introducing genetic changes into food organisms that are more predictable than those introduced through conventional breeding techniques. This review discusses whether the consumption of DNA in approved novel foods and novel food ingredients derived from genetically modified organisms (GMOs) can be regarded as being as safe as the consumption of DNA in existing foods. It concludes that DNA from GMOs is equivalent to DNA from existing food organisms that has always been consumed with human diets. Any risks associated with the consumption of DNA will remain, irrespective of its origin, because the body handles all DNA in the same way. The breakdown of DNA during food processing and passage through the gastrointestinal tract reduces the likelihood that intact genes capable of encoding foreign proteins will be transferred to gut microflora. The review does not specifically address food safety issues arising from the consumption of viable genetically modified microorganisms but it shows that the likelihood of transfer and functional integration of DNA from ingested food by gut microflora and/or human cells is minimal. Information reviewed does not indicate any safety concerns associated with the ingestion of DNA per se from GMOs resulting from the use of currently available recombinant DNA techniques in the food chain. [less ▲]

Risk assessment of antibiotic resistance markers in genetically modified crops

Scientific Conference (2000)

Comparison of the EU and the U.S. regulatory framework for the environmental safety assessment of transgenic crops - an industry perspective

Scientific Conference (1998)

The pipecolate-incorporating enzyme for the biosynthesis of the immunosuppressant rapamycin: Nucleotide sequence analysis, disruption and heterologous expression of rapP from Streptomyces hygroscopicus.

in European Journal of Biochemistry (1997), 247(2), 526-534

An open reading frame (rapP) encoding the putative pipecolate-incorporating enzyme (PIE) has been identified in the gene cluster for the biosynthesis of rapamycin in Streptomyces hygroscopicus. Conserved ... [more ▼]

An open reading frame (rapP) encoding the putative pipecolate-incorporating enzyme (PIE) has been identified in the gene cluster for the biosynthesis of rapamycin in Streptomyces hygroscopicus. Conserved amino acid sequence motifs for ATP binding, ATP hydrolysis, adenylate formation, and 4'-phosphopantetheine attachment were identified by sequence comparison with authentic peptide synthetases. Disruption of rapP by phage insertion abolished rapamycin production in S. hygroscopicus, and the production of the antibiotic was specifically restored upon loss of the inserted phage by a second recombination event. rapP was expressed in both Escherichia coli and Streptomyces coelicolor, and recombinant PIE was purified to homogeneity from both hosts. Although low-level incorporation of [14C]beta-alanine into recombinant PIE isolated from E. coli was detected, formation of the covalent acylenzyme intermediate could only be shown with the PIE from S. coelicolor, suggesting that while the recombinant PIE from S. coelicolor was phosphopantetheinylated, only a minor proportion of the recombinant enzyme from E. coli was post-translationally modified. [less ▲]

Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of the enzymatic domains in the modular polyketide synthase

in Gene (1996), 169(1), 9-16

The three giant multifunctional polypeptides of the rapamycin (Rp)-producing polyketide synthase (RAPS1, RAPS2 and RAPS3) have recently been shown to contain 14 separate sets, or modules, of enzyme ... [more ▼]

The three giant multifunctional polypeptides of the rapamycin (Rp)-producing polyketide synthase (RAPS1, RAPS2 and RAPS3) have recently been shown to contain 14 separate sets, or modules, of enzyme activities, each module catalysing a specific round of polyketide chain extension. Detailed sequence comparison between these protein modules has allowed further characterisation of aa that may be important in catalysis or specificity. The acyl-carrier protein (ACP), beta-ketoacyl-ACP synthase (KS) and acyltransferase (AT) domains (the core domains) have an extremely high degree of mutual sequence homology. The KS domains in particular are almost perfect repeats over their entire length. Module 14 shows the least homology and is unique in possessing only core domains. The enoyl reductase (ER), beta-ketoacyl-ACP reductase (KR) and dehydratase (DH) domains are present even in certain modules where they are not apparently required. Four DH domains can be recognised as inactive by characteristic deletions in active site sequences, but for two others, and for KR and ER in module 3, the sequence is not distinguishable from that of active counterparts in other modules. The N terminus of RAPS1 contains a novel coenzyme A ligase (CL) domain that activates and attaches the shikimate-derived starter unit, and an ER activity that may modify the starter unit after attachment. The sequence comparison has revealed the surprisingly high sequence similarity between inter-domain 'linker' regions, and also a potential amphipathic helix at the N terminus of each multienzyme subunit which may promote dimerisation into active species. [less ▲]

Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases.

in FEBS Letters (1995), 374(2), 246-248

The amino acid sequences of a large number of polyketide synthase domains that catalyse the transacylation of either methylmalonyl-CoA or malonyl-CoA onto acyl carrier protein (ACP) have been compared ... [more ▼]

The amino acid sequences of a large number of polyketide synthase domains that catalyse the transacylation of either methylmalonyl-CoA or malonyl-CoA onto acyl carrier protein (ACP) have been compared. Regions were identified in which the acyltransferase sequences diverged according to whether they were specific for malonyl-CoA or methylmalonyl-CoA. These differences are sufficiently clear to allow unambiguous assignment of newly-sequenced acyltransferase domains in modular polyketide synthases. Comparison with the recently-determined structure of the malonyltransferase from Escherichia coli fatty acid synthase showed that the divergent region thus identified lies near the acyltransferase active site, though not close enough to make direct contact with bound substrate. [less ▲]

Cloning of structural genes for type I polyketide synthases involved in macrolide polyether biosynthesis

Scientific Conference (1994)