Post-translational modifications (PTMs) are widely employed by all living organisms to control the enzymatic activity, localization or stability of proteins on a much shorter time scale than the transcriptional control. In eukarya, global analyses consistently reveal that proteins are very extensively phosphorylated, acetylated and ubiquitylated. Glycosylation and methylation are also very common, and myriad other PTMs, most with a proven regulatory potential, are being discovered continuously. The emergent picture is that PTM sites on a single protein are not independent; modification of one residue often affects (positively or negatively) modification of other sites on the same protein. The best example of this complex behavior is the histone “bar-code” with very extensive cross-talk between phosphorylation, acetylation and methylation sites. Traditionally it was believed that large networks of PTMs exist only in complex eukaryal cells, which exploit them for coordination and fine-tuning of various cellular functions. PTMs have also been detected in bacteria, but the early examples focused on a few important regulatory events, based mainly on protein phosphorylation. The global importance (and abundance) of PTMs in bacterial physiology was systematically underestimated. In recent years, global studies have reported large datasets of phosphorylated, acetylated and glycosylated proteins in bacteria. Other modifications of bacterial proteins have been recently described: pupylation, methylation, sirtuin acetylation, lipidation, carboxylation and bacillithiolation. As the landscape of PTMs in bacterial cells is rapidly expanding, primarily due to advances of detection methods in mass spectrometry, our research field is adapting to comprehend the potential impact of these modifications on the cellular physiology. The field of protein phosphorylation, especially of the Ser/Thr/Tyr type, has been profoundly transformed. We have become aware that bacterial kinases phosphorylate many protein substrates and thus constitute regulatory nodes with potential for signal integration. They also engage in cross-talk and eukaryal-like mutual activation cascades. The regulatory potential of protein acetylation and glycosylation in bacteria is also rapidly emerging, and the cross-talk between acetylation and phosphorylation has been documented. This topic deals with the complexity of the PTM landscape in bacteria, and focus in particular on the physiological roles that PTMs play and methods to study them. The topic is associated to the 1st International Conference on Post-Translational Modifications in Bacteria (September 9-10, 2014, Göttingen, Germany).

Post-translational modifications serve many different purposes in several cellular processes such as gene expression, protein folding and transport to appropriate cell compartment, protein-lipid and protein-protein interactions, enzyme regulation, signal transduction, cell proliferation and differentiation, protein stability, recycling and degradation. Although several-hundred different modifications are known, the significance of many of them remains unknown. The enormous versatility of the modifications which frequently alter the physico-chemical properties of the respective proteins represents an extraordinary challenge in understanding their physiological role. Since essential cellular functions are regulated by protein modifications, an improvement of current understanding of their meaning might allow new avenues to prevent and/or alleviate human and animal diseases.

A cofactor is a component part of many enzymes and functions by uniting with another molecule in order to become active. The use of cofactors to supplement the native amino acids of a protein is essential to maintain the chemical capabilities necessary for organisms to survive. This volume focuses on the significant advances of the past decade in identifying and describing new cofactors--either small molecules or those derived posttranslationally.

How the amino acid sequence of a protein determines its three-dimensional structure is a major problem in biology and chemistry. Leading experts in the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling offer provocative insights into current views on the protein folding problem and various aspects for future progress.

Lipid Modification of Proteins: A Practical Approach is a unique guide to the latest methods is use, written by the acknowledged experts in the field. Detailed protocols are provided for all the key techniques, and the relevant background material is included. This book is an essential manual for a wide range of scientists studying the modification of protein by lipids, including membrane and protein biochemists, cell biologists, immunologists, bacteriologists, parasitologists, and virologists.

Corynebacterium glutamicum was discovered in Japan in 1956 as a natural glutamate producer. Its “microbial factory” qualities, such as its physiological plasticity and robust catalytic functionalities, have since facilitated the development of efficient production processes for amino acids, nucleotides and vitamins. This monograph illustrates how the information gleaned from complete genome sequencing allows the rational engineering of the entire cellular metabolism and how systems biology permits the further optimization of C. glutamicum as a biocatalyst. Aspects of gene regulation, metabolic pathways, sugar uptake, protein secretion, cell division and biorefinery applications highlight the enormous biotechnological and biorefinery potential.