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The Role of AAA+ Proteins in Protein Repair and Degradation
ATPases Associated with diverse cellular Activities (AAA+) comprise a superfamily of proteins that are defined by the presence of the AAA+ domain containing canonical Walker A and B motifs required for ATP binding and hydrolysis. Members of this superfamily act on other proteins, DNA, RNA, or multicomponent complexes to affect their conformation or their assembly. There have been substantial advances in understanding the structure and mechanism of function of a large number of AAA+ proteins. In this Research Topic, review articles and original research papers discuss new aspects as well as provide a detailed overview of several AAA+ proteins, namely: ClpXP, Lon, ClpB, Hsp104, p97, AAA+ proteins of the proteasome, Rubisco activases, Torsin, Pontin, and Reptin.
The Molecular Chaperones Interaction Networks in Protein Folding and Degradation
Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved i...
Prokaryotic Systems Biology
This book focuses on innovative experimental and computational approaches for charting interaction networks in bacterial species. The first part of the volume consists of nine chapters, focusing on biochemical and genetics and genomics approaches including yeast two hybrid, metagenomics, affinity purification in combination with mass spectrometry, chromatin-immunoprecipitation coupled with sequencing, large-scale synthetic genetic screens, and quantitative-based mass spectrometry strategies for mapping the bacterial physical, functional, substrate, and regulatory interaction networks needed for interpreting biological networks, inferring gene function, enzyme discovery, and identifying new d...
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
This book makes a novel synthesis of the molecular aspects of the stress response and long term adaptation processes with the system biology approach of biological networks. Authored by an exciting mixture of top experts and young rising stars, it provides a comprehensive summary of the field and identifies future trends.
Mitochondria in Health and in Sickness
Besides bringing together researchers and clinicians from various disciplines to share their scope of research on the seminal role of mitochondria in human disease, this original volume of the book has a broader appeal by exploring the health and disease of mitochondria, with specific emphasis on how mitochondrial dysfunction contributes to the development of various neurodegeneration, cancer, and metabolic disorders. The book also provides a foundational overview of the mitochondrial pathogenic or genetic variants and highlights various analytical tools used in the field of mitochondrial genetics; mitochondrial replacement therapy and strategies geared towards shifting heteroplasmy in indiv...
Functions and Mechanisms of Bacterial Protein Homeostasis and Stress Responses
The Cover Image for This Research Topic is Used With Permission of the Authors and Publishers of the Following Article: Winkler J, Seybert A, König L, Pruggnaller S, Haselmann U, Sourjik V, Weiss M, Frangakis AS, Mogk A, Bukau B.EMBO J. 2010 Mar 3;29(5):910-23. doi: 10.1038/emboj.2009.412. Epub 2010 Jan 21
Heat Shock Proteins of Malaria
This book describes the role of heat shock proteins in the life cycle of malaria parasites. The work includes a general introduction on the structural and functional features of heat shock proteins. The main focus is on the role of heat shock protein families from Plasmodium falciparum, their role in protein folding and in the development of malaria pathology. The functions of individual families of heat shock proteins from plasmodium species and their cooperation in functional networks is described. Subcellular and extracellular organelles such as the apicoplast and the Maurer’s Clefts which are associated with plasmodium species, are discussed in detail. The role of heat shock proteins in the development and function of these organelles structures are highlighted. Although conceding that heat shock proteins may not be ideal antimalarial drug targets, prospects of targeting heat shock proteins in antimalarial drug discovery either directly and/or in combination therapies are explored.
Prefoldins: the new chaperones
This book reviews recent work on molecular chaperones of the prefoldin family from their discovery in Archaea to the basic clarification of their structure. Even though, there is still a lot to investigate in order to understand the roles and functions of prefoldins, some preliminary work suggests their contribution in assembly and activation of a variety of macromolecular complexes. Hence, the reader is introduced to recent structural findings via cryo-electron microscopy and to the importance of this particular group of proteins in health and disease. This book also discusses the particular structure of the URI prefoldin-like complex. In addition, recent developments in the generation of URI mouse models speculate on the functions and emerging roles of the URI prefoldin-like complex in various cellular processes. This novel protein complex represents a unique cellular machinery, which molecular basis of its activity still remains to be determined. This work is thus a guide to help researchers in the field to have a more comprehensive and critical view of the prefoldin world.
Type I Chaperonins: Mechanism and Beyond
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.
