The Chaperonins

The first of its kind, this volume presents the latest research findings on the chaperonins, the best studied family of a class of proteins known as molecular chaperones. These findings are changing our view of some fundamental cellular processes involving proteins, especially how proteins fold into their functional conformations. Origins of the new view of protein folding Prokaryotic chaperonins Eukaryotic chaperonins Evolution of the chaperonins Refolding of denatured proteins Organelle biosynthesis Biomedical aspects

This book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field. It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology – more specifically, in protein folding pathways.

Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.

This book reviews understanding of the biological roles of extracellular molecular chaperones. It provides an overview of the structure and function of molecular chaperones, their role in the cellular response to stress and their disposition within the cell. It also questions the basic paradigm of molecular chaperone biology - that these proteins are first and foremost protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving concept of proteins (such as molecular chaperones) as multi-functional molecules for which the term 'moonlighting proteins' has been introduced is discussed. The role of exogenous molecular chaperones as cell regulators is examined and the physiological and pathophysiological role that molecular chaperones play is described. In the final section, the potential therapeutic use of molecular chaperones is described and the final chapter asks the question - what does the future hold for the extracellular biology of molecular chaperones?

Type I chaperonins are key players in maintaining the proteome of bacteria and organelles of bacterial origin. They are well known for their crucial role in mediating protein folding. For almost three decades, the molecular mechanism of chaperonin function has been the subject of intensive research. Still, surprising new mechanistic discoveries are constantly reported. It seems that we are far from having a full understanding of the chaperonin mode of action. Chaperonins are not simply protein folding machines. They also perform diverse extramitochondrial tasks, mainly related to inflammatory and signal transduction processes. This eBook constitutes ten articles highlighting the latest developments related to the divers functions of Type I chaperonins. As its title, mechanism and beyond, the collection starts with mechanistic view, continues with extracellular functions and ends with biotechnological applications of Type I chaperonins.

Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.

The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological functions, the development of ligand-based structural complexes and the consequent pharmacological or biotechnological applications of these processes. The involvement of molecular chaperones in several processes ranging from regulation of transcription factors and protein-protein interactions in bacteria to proteostasis, signaling pathways and cancer are also addressed. The book is an essential consulting tool for researchers, working professionals in academia or industry, and students of all levels who wish to obtain the most relevant and updated information currently available about protein folding and chaperones.

In this text, leading experts synthesise our body of knowledge , and the reader gains not only a fuller understanding of the roles of chaperones in the context of cellular processes, but also an insight into the nature of these proteins.