Plant thioredoxins: the multiplicity conundrum

Thioredoxins are small proteins distinguished by the presence of a conserved dicysteine active site. In oxidized thioredoxin, the two cysteines form a disulfide bond that is targeted by the enzyme thioredoxin reductase. Together with an electron donor, thioredoxin and thioredoxin reductase form the 'thioredoxin system' that is present in all organisms. Thioredoxins participate in dithiol/disulfide exchange reactions with a large range of cellular substrates. Higher plants possess a very complex thioredoxin profile consisting of at least two different thioredoxin systems that contain distinct, multigenic thioredoxin classes which have different intracellular localizations. In this review we summarise the current state of knowledge regarding the function of plant thioredoxins representing all systems and classes. Received 30 October 2001; received after revision 13 December 2001; accepted 17 December 2001     

Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum

The biosynthesis of cobalamin (vitamin B12) is described, revealing how the concerted action of around 30 enzyme-mediated steps results in the synthesis of one of Nature's most structurally complex 'small molecules'. The plethora of genome sequences has meant that bacteria capable of cobalamin synthesis can be easily identified and their biosynthetic genes compared. Whereas only a few years ago cobalamin synthesis was thought to occur by one of two routes, there are apparently a number of variations on these two pathways, where the major differences seem to be concerned with the process of ring contraction. A comparison of what is currently known about these pathways is presented. Finally, the process of cobalt chelation is discussed and the structure/function of the cobalt chelatase associated with the oxygen-independent pathway (CbiK) is described.     

Introduction: the ribonuclease A superfamily

In this multi-author issue several aspects of the ribonuclease A superfamily are reviewed. This superfamily can be subdivided in a number of mammalian and other vertebrate ribonuclease families. In the introduction chapter the titles of the other contributions are presented. There is little uniformity in the nomenclature of ribonucleases, caused in part by gene duplications, which have occurred independently in several mammalian lineages, and which are nice examples for explaining orthology and paralogy in molecular evolution.     

Introduction: Structuralists of the world unite

Key arguments and claims in Steven French's The Structure of the World are articulated and assessed. Differences between different forms of ontic structural realism are articulated, and some problems raised for some aspects of French's version.     

Anticarcinogenic effects of selenium

Selenium (Se) exerts its anticarcinogenic effects by multiple mechanisms. In the physiological dosage range, Se appears to function as an antimutagenic agent, preventing the malignant transformation of normal cells and the activation of oncogenes. These protective effects of Se seem to be primarily associated with its presence in the glutathione peroxidases, which are known to protect DNA and other cellular components from damage by oxygen radicals. Selenoenzymes are also known to play roles in carcinogen metabolism, in the control of cell division, oxygen metabolism, detoxification processes, apoptosis induction and the functioning of the immune system. Other modes of action, either direct or indirect, may also be operative, such as the partial retransformation of tumor cells and the inactivation of oncogenes. However, the effects of Se in the physiological dosage range are not attributable to cytotoxicity, allowing Se to be defined as a genuine nutritional cancer-protecting agent. The anticarcinogenic effects of Se are counteracted by Se-antagonistic compounds and elements. For maximal utilization of its cancer-protective potential, Se supplementation should start early in life and be maintained over the entire lifespan. In addition, exposure to Se antagonists and carcinogenic risk factors should be minimized by appropriate dietary and lifestyle changes.     

Introduction: Reappraising Paul Feyerabend

This volume is devoted to a reappraisal of the philosophy of Paul Feyerabend. It has four aims. The first is to reassess his already well-known work from the 1960s and 1970s in light of contemporary developments in the history and philosophy of science. The second is to explore themes in his neglected later work, including recently published and previously unavailable writings. The third is to assess the contributions that Feyerabend can make to contemporary debate, on topics such as perspectivism, realism, and political philosophy of science. The fourth and final aim is to reconsider Feyerabend's place within the history of philosophy of science in the light of new scholarship.     

Introduction: lipid-binding proteins: novel aspects

Lipid-binding proteins function to transport lipids across membranes and aqueous phases and act to solubilise their cargo, protect it from chemical damage and probably also to define its destination. As such, they have been adapted to carry out a broad spectrum of biological functions in addition to their classical roles in energy metabolism and the transmission or blocking of retinoid-based signalling. The set of reviews in this issue of CMLS is designed to draw attention to some newly understood aspects and principles of their biology and structure, and concentrates on the proteins involved in transport of fatty acids and retinoids.