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This article (part I of a two-part paper) presents results of a substance abuse treatment training needs assessment study conducted with 133 nurses who were working in randomly selected New England substance abuse treatment facilities. This sample of nurses was derived from a larger survey sample of 1684 substance abuse treatment providers working in randomly selected New England substance abuse treatment facilities. These needs assessment data show that, compared with drug and alcohol counselors, social workers, and physicians or residents, nurses have the lowest levels of skill or knowledge in 8 of 12 substance abuse-specific treatment areas. Nurses reported that additional training would increase their clinical effectiveness. Without adequate training, nurses cannot fulfill their roles in prevention, intervention and treatment.

This article (part II of a two-part paper) presents the results of a substance abuse treatment training needs assessment study conducted with 133 nurses who were working in randomly selected New England substance abuse treatment facilities. This sample of nurses was derived from a larger survey sample of 1684 substance abuse treatment providers working in randomly selected New England substance abuse treatment facilities. These needs assessment data show that, compared with drug and alcohol counselors, social workers, and physicians or residents, nurses had the highest levels of training need in the three major substance abuse treatment domains investigated in this study. Without training, nurses cannot fulfill their roles in prevention, intervention and treatment. Agencies and institutions concerned with and committed to training health care providers are encouraged to attend to the demonstrated need for training while interest is high and clinical demand is great.

The Saccharomyces cerevisiae protein MSS4 is essential and homologous to mammalian phosphatidylinositol-4-phosphate (PI(4)P) 5-kinases. Here, we demonstrate that MSS4 is a lipid kinase. MSS4 has dual substrate specificity in vitro, converting PI(4)P to PI(4, 5)P2 and to a lesser extent PI(3)P to PI(3,4)P2; no activity was detected with PI or PI(5)P as a substrate. Cells overexpressing MSS4 contain an elevated level specifically of PI(4,5)P2, whereas mss4 mutant cells have only approximately 10% of the normal amount of this phosphorylated phosphoinositide. Furthermore, cells lacking MSS4 are unable to form actin cables and to properly localize their actin cytoskeleton during polarized cell growth. Overexpression of RHO2, encoding a Rho-type GTPase involved in regulation of the actin cytoskeleton, restores growth and polarized distribution of actin in an mss4 mutant. These results suggest that MSS4 is the major PI(4)P 5-kinase in yeast and provide a link between phosphoinositide metabolism and organization of the actin cytoskeleton in vivo.

We are studying the molecular mechanism of cellular protein localization. The availability of genetic techniques, such as gene fusion in Escherichia coli, has made this problem particularly amenable to study in this prokaryote. We have constructed a variety of strains in which the gene coding for an outer membrane protein is fused to the gene coding for a normally cytoplasmic enzyme, beta-galactosidase. The hybrid proteins produced by such strains retain beta-galactosidase activity; this activity serves as a simple biochemical tag for studying the localization of the outer membrane protein. In addition, we have exploited phenotypes exhibited by certain fusion strains to isolate mutants that are altered in the process of protein export. Genetic and biochemical analyses of such mutants have provided evidence that the molecular mechanism of cellular protein localization is strinkingly similar in both bacteria and animal cells.

The lamB701-708 signal sequence mutation reduces expression of LamB, an outer membrane protein of Escherichia coli. To investigate the possibility that synthesis and export of LamB are coupled, as suggested by the expression defect of the lamB701-708 mutation, we isolated intragenic suppressors of the lamB701-708 mutation. The expression defect imposed by the lamB701-708 mutation is suppressed by an export-defective signal sequence mutation, suggesting that translation and export are coupled. The additional observation that not all export-defective signal sequence mutations suppressed the lamB701-708 expression defect suggests that translational arrest can be uncoupled from export.

We report here on the cloning of a gene located within the ompB locus of E. coli K-12. This gene, designated ompR, resides on a 10.9-kilobase EcoRI fragment that we cloned, using a lambda vector and in vitro packaging techniques. By subcloning portions of this fragment into the high-copy-number plasmid pBR322, we have isolated the ompR gene on a 1.4-kilobase EcoRI-AvaI fragment. This fragment has been characterized physically and will facilitate a more detailed study of the role and mechanism of porin regulation by the ompB locus.