Genetic selection for reproductive photoresponsiveness in deer mice

Seasonal breeding is common in mammals, particularly in habitats outside the tropics. Climate and availability of food are the ultimate factors that usually dictate the optimal time of year for a mammal to breed; however, day length (photoperiod) often serves as the proximal cue to signal the onset or cessation of seasonal reproduction. Some individuals in some populations of deer mice are reproductively responsive to photoperiod, while other individuals in the same population are not. As shown here, selection can dramatically alter the frequency of photoresponsiveness in a laboratory population in only two generations. To our knowledge this is the first demonstration of selection for reproductive photoresponsiveness in any mammal. By implication, some wild populations of deer mice must use multiple, genetic-based reproductive strategies, and the degree to which each such strategy is exhibited must be subject to rapid change in response to both seasonally and momentarily changing climatic and dietary conditions.     

Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)

There have been many reports that eukaryotic cells contain ring-shaped 19S or 20S particles which are composed of numerous polypeptide subunits ranging in size between 25 and 35 kilodaltons. Because these particles seemed to copurify with inactive mRNA, they were assumed to function in regulating mRNA translation and hence were named 'prosomes' (for 'programmed-o-some'). A number of properties have been reported for these structures, including an association with specific RNA species or with certain heat-shock proteins and involvement in tRNA processing or aminoacyl tRNA synthesis. However, these proposed activities have not been supported by definitive evidence. During studies of the proteolytic systems in mammalian tissues, we noted many similarities between these 19S particles and the high molecular weight protease complexes that are present in most or all eukaryotic cells. This (700 kilodalton) enzyme complex, designated here as LAMP for 'large alkaline multi-functional protease', contains three distinct endoproteolytic sites which function at neutral or alkaline pH and are specific for hydrolysis of proteins, hydrophobic peptides, or basic peptides. This protease also exists in a latent form which can be activated by polylysine, fatty acids, or ATP. In this report, we show that the prosomes and these protease complexes are very similar or identical with respect to their size, polypeptide composition, immunological cross-reactivity, appearance in the electron microscope, radial symmetry of subunits, subcellular localization, and proteolytic activities. Therefore, the 'prosome' probably plays a critical role in intracellular protein breakdown, and we propose that it be renamed 'proteasome'.