Preface
The cell envelope of Gram-negative bacteria, including the plasma membrane, the periplasmic space, and the outer membrane, can be viewed as a model organelle with a large number of diverse critical functions for bacterial physiology. A significant number of protein structures of both the inner and outer membrane, as well as proteins from the periplasm, have been solved by NMR or X-ray at an increasing rate over the past few years. Proteomics techniques have begun to make it possible to obtain a detailed inventory of the contents of the cell envelope of Gram-negative bacteria. The methods and data are now maturing to provide information about the interactions between the different proteins and other biomolecules. Biochemical and biophysical approaches have given a great deal of information about the cellular processes occurring in the envelope, including bioenergetics, transport, signaling, cell wall synthesis, and various other catalytic activities.
The contributions in this special issue provide a timely review of major aspects of the envelope components with known structures and their environment. They complement the more microbiological approach in a recent book. The degree of detail in our current understanding of the cell envelope and its processes suggests the cell envelope may become one of the first organelles that is sufficiently studied and understood to create computational models with predictive powers at a cellular level.
Several reviews focus on individual classes of proteins, e.g., mechanosensitive channels and ABC transporters; others focus on functional systems, such as the iron import cascade, protein secretion systems and the flagellar assembly; while yet others review the state of the art in methodological developments in crystallography, proteomics, and computational investigations in membrane proteins.
We thank the authors of all contributions for their efforts.
D. Peter Tieleman
Peter Tieleman studied chemistry and philosophy at the University of Groningen van 1990-1995. He was a graduate student in the group of Prof. Herman Berendsen from 1995 to 1998 when he completed his PhD degree in biophysical chemistry. After an EMBO postdoctoral fellowship with Prof. Mark Sansom at the University of Oxford he joined the University of Calgary in 2000 as Assistant Professor and Scholar of the Alberta Heritage Foundation for Medical Research (AHFMR). He is currently Professor of Biochemistry, AHFMR Senior Scholar, and a New Investigator of the Canadian Institutes for Health Research. Tieleman and his group are interested in the biophysics of lipids and membrane proteins. The group uses and develops computational methods to study a range of problems, including lipid structure, membrane perturbations, transport proteins, and lung surfactant. He is on the editorial board of several journals, including Biophysical Journal and BBA.
Raymond J. Turner
Raymond J. Turner did his undergraduate studies in chemistry and biochemistry obtaining a BSc in 1985 from the University of Calgary. He then continued in Calgary studying dynamics of proteins by time-resolved fluorescence obtaining his PhD in physical biochemistry in 1990. From there he went to the University of Alberta to learn molecular microbiology and study resistance mechanisms with Dr. Diane Taylor. He continued as an AHFMR postdoctoral fellow working between Drs. Taylor and Joel Weiner, in the Biochemistry department, leading him towards an interest in membrane proteins. He was recruited back to the University of Calgary in 1998 as an assistant professor in the department of biological sciences, faculty of science. He received an AHFMR establishment grant for work on membrane proteins in 1999. He is currently Professor of Biochemistry and Chair of the Biomolecules/ Cells/ Microbes research cluster of the department. His research interests span from: developing protein chemistry tools through modification of indol; proteomic and bioinformatic analysis of protein maturation systems; folding and ligand binding of integral membrane proteins, particularly multidrug resistance proteins; system specific chaperones for the twin-arginine translocase in bacteria; and multimetal resistance and tolerance mechanisms in bacteria. Recent recognitions include a Senior Visiting Fellowship in 2007, at the Institute of Advanced Study, University of Bologna, Italy.
Hans J. Vogel
Hans J. Vogel is a Professor of Biochemistry and an AHFMR Scientist in the Department of Biological Sciences at the University of Calgary. He is the Director of the local Biophysical Characterization Facility, the Bio-NMR Centre and the associated Metabolomics Research Centre. He received his original academic training at the University of Groningen, the Netherlands, the University of Alberta in Edmonton, Canada and the University of Lund in Sweden. He joined the University of Calgary in 1985 and was promoted to full professor in 1991. His research work has mostly focused on the use of NMR spectroscopy for the study of metalloproteins, particularly those involved in calcium-regulatory mechanisms, such as calmodulin, as well as mammalian proteins that mediate the transport of iron and copper. In addition, bacterial iron uptake pathways are being studied as they offer opportunities for the development of novel antibiotics. Dr. Vogel has also contributed immensely to our understanding of the role of antimicrobial peptides and related host-defense proteins in innate immunity. Early in his career he has worked on in vivo NMR spectroscopy of living animals and this has allowed his group to successfully contribute to the emerging metabolomics field. To date Dr. Vogel has published more than 300 scientific papers and he is currently a member of the Editorial Board of five journals. He is a regularly invited speaker at major international and national conferences and he has won several research awards.
Dr. Joel Weiner
Dr. Joel Weiner is a University Professor. He served as Associate Dean, Research for the Faculty of Medicine and Dentistry, University of Alberta from 1993 -2005. Dr. Weiner’s research is focused on the regulation, synthesis, assembly, function and structure of E. coli membrane-bound energy conserving enzymes. He has published over 180 peer-reviewed papers in the area and has made major contributions to our understanding of membrane protein assembly and translocation, cofactor biosynthesis, subunit-subunit communication in complex membrane-bound enzymes and the role of electron transfer relays in complex oxidation-reduction enzymes. Dr. Weiner was the past Director of the Medical Research Council Group in the Molecular Biology of Membrane Proteins and PI of Project CyberCell a major initiative funded by the Canada Foundation for Innovation and partners.
Dr. Weiner has served the community through service on editorial boards, grant review panels, presidency of the Canadian Society for Biochemistry, Molecular Biology and Cell Biology as well as the Council of the Medical Research Council (1996-2000) and Council of Scientists of the Human Frontiers Science Program (1998-2001). Dr. Weiner has organized several international meetings and was President of the 19th International Congress of Biochemistry and Molecular Biology. Dr. Weiner has received the Killam Annual Professorship and the Distinguished Service award of the International Union for Biochemistry & Molecular Biology.
