Building a Community Through Workplace E-Mail: The New Privacy Frontier

The relatively new technology of electronic mail (e-mail) presents an entirely new issue of workplace privacy. Currently, whether a person has a privacy interest in their workplace e-mail communications is as unsettled an issue as it has been since the technology emerged in the early part of this decade as the preferred mode of communication in the workplace. Indeed, e-mail may soon be the preferred mode of communication in general. This comment will argue that all e-mail users have a privacy interest in workplace e-mail communications and that the current law does not afford e-mail users any type of protection for this interest. Part I will address the rise of e-mail in the workplace and the privacy interest users have in their workplace e-mail. Part II will discuss the law currently in existence that has been applied to workplace e-mail privacy and how this body of law has failed to recognize a privacy interest in workplace e-mail messages. Part III will discuss the few solutions that have been proposed to deal with workplace e-mail privacy and how these fall far short of protecting this important privacy interest. This comment will then propose a structure of federal legislation to address this issue, concluding that e-mail in the workplace should be a protected privacy interest and that federal legislation is the only way in which to protect this interest

Turnover of outer and inner membrane proteins of rat liver mitochondria

Recent reports on the properties and composition of outer and inner mitochondrial membranes suggest that outer and inner membranes of mitochondria are derived from different sources of the cell [l-3]. I

Sites of Biosynthesis of Outer and Inner Membrane Proteins of Neurospora crassa Mitochondria

Outer and inner membranes of Neurospora crassa mitochondria were separated by the combined swelling, shrinking, sonication procedure. Membranes were characterized by electron microscopy and by marker enzyme activities. A red carotenoid pigment was found to be concentrated in the outer membrane. The inner mitochondrial membrane was resolved into about 20 protein bands on polyacrylamide gel electrophoresis, whereas the outer membrane shows essentially one single protein band. Only negligible incorporation of radioactive amino acids occurs into outer membrane when isolated mitochondria are synthesizing polypeptide chains. In agreement with this observation labeling of outer membrane protein is almost entirely blocked, when whole Neurospora cells are incubated with radioactive amino acids in the presence of cycloheximide, an inhibitor of cytoplasmic protein synthesis. Finally, the essential electrophoretic protein band from outer membrane does not become labeled when mitochondria are incubated with radioactive amino acids either in vitro or in vivo in the presence of cycloheximide. It is concluded that the vast majority, if not all, of the outer membrane protein is synthesized by the cytoplasmic system and that polypeptide chains formed by the mitochondrial ribosomes are integrated into the inner mitochondrial membrane

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

The Fe/S protein of complex III is encoded by a nuclear gene, synthesized in the cytoplasm as a precursor with a 32 residue amino-terminal extension, and transported to the outer surface of the inner mitochondrial membrane. Our data suggest the following transport pathway. First, the precursor is translocated via translocation contact sites into the matrix. There, cleavage to an intermediate containing an eight residue extension occurs. The intermediate is then redirected across the inner membrane, processed to the mature subunit, and assembled into complex III. We suggest that the folding and membrane-translocation pathway in the endosymbiotic ancestor of mitochondria has been conserved during evolution of eukaryotic cells; transfer of the gene for Fe/S protein to the nucleus has led to addition of the presequence, which routes the precursor back to its “ancestral” assembly pathway