Preface
The High Mobility Group (HMG) proteins were first isolated from the nuclei of mammalian cells and named according to their electrophoretic mobility. Subsequently, the HMGs were subdivided into 3 families named HMGA, HMGB, and HMGN [1]. Although all “canonical” HMGs share certain physical characteristics and all bind to chromatin, the 3 families are structurally distinct and perform unique functions. Each HMG family has a characteristic functional sequence motif: the functional motif of the HMGA family is named the “AT-hook,” that of the HMGB family is named the “HMG-box,” and that of HMGN family is named “the nucleosomal binding domain.” Information on the nomenclature of the HMGs can be found at “http://www.informatics.jax.org/mgihome/nomen/hmg_family.shtml”. The functional motifs of the HMGs are embedded in many nuclear proteins alongside additional motifs. These proteins are known as “HMG-motif proteins.” The reviews in this issue pertain specifically to the “canonical” HMGs and do not provide information on the HMG-motif proteins.
Michael Bustin
Michael Bustin Ph.D., is a Senior Investigator and Chief of the Protein Section at the National Cancer Institute, NIH. He received his Ph.D. from the University of California, Berkeley, where he studied the structure and biological activity of the linker histone H1. Following a postdoctoral fellowship at Rockefeller Institute under the guidance of the Nobel laureates S. Moore and W.H. Stein, he joined the department of Chemical Immunology at the Weizmann Institute of Science, Israel, where he generated antibodies to histones and HMGs and pioneered the use of immunochemical approaches for studies on chromatin structure and function. His current research interests center on the structure and function of HMG proteins and on the molecular mechanisms whereby events occurring in chromatin affect the cellular phenotype.
