There has been an influx of immigrants from El Salvador to the Washington, DC (DC) area, but little is known about the health behaviors of this population. This study was conducted to describe the prevalence of cigarette smoking among adult Salvadorean immigrants to the DC area. Bilingual interviewers administered a face-to-face interview to participants recruited from throughout the community. Complete data were available for 1,458 participants: 10.8% of those surveyed were current smokers and 11.7% were former smokers. Men were significantly more likely than women to have ever smoked either in the past (adjusted prevalence difference [PD = 21.0%] or currently (PD = 21.2%). The respondents tended to believe that smoking was a "habit" rather than an addition. Only 16% lived in households where smoking was permitted, and the majority supported smoke-free policies in public places, with men and current smokers being less permissive. The smoking behavior exclusively represented the smoking pattern that the Salvadoreans had adopted before immigration. The data suggest that smoking control strategies aimed at this population should seek to reduce the onset of smoking among men and continue to keep smoking among women rare.
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This review focuses on organellar AAA/FtsH proteases, whose proteolytic and chaperone-like activity is a crucial component of the protein quality control systems of mitochondrial and chloroplast membranes. We compare the AAA/FtsH proteases from yeast, mammals and plants. The nature of the complexes formed by AAA/FtsH proteases and the current view on their involvement in degradation of non-native organellar proteins or assembly of membrane complexes are discussed. Additional functions of AAA proteases not directly connected with protein quality control found in yeast and mammals but not yet in plants are also described shortly. Following an overview of the molecular functions of the AAA/FtsH proteases we discuss physiological consequences of their inactivation in yeast, mammals and plants. The molecular basis of phenotypes associated with inactivation of the AAA/FtsH proteases is not fully understood yet, with the notable exception of those observed in m-AAA protease-deficient yeast cells, which are caused by impaired maturation of mitochondrial ribosomal protein. Finally, examples of cytosolic events affecting protein quality control in mitochondria and chloroplasts are given. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids. Copyright 2012 Elsevier B.V. All rights reserved.
ATPases Associated with various cellular Activities (AAA+ ATPases) are molecular motors that use the energy of ATP binding and hydrolysis to remodel their target macromolecules. The majority of these ATPases form ring-shaped hexamers in which the active sites are located at the interfaces between neighboring subunits. Structural changes initiate in an active site and propagate to distant motor parts that interface and reshape the target macromolecules, thereby performing mechanical work. During the functioning cycle, the AAA+ motor transits through multiple distinct states. Ring architecture and placement of the catalytic sites at the intersubunit interfaces allow for a unique level of coordination among subunits of the motor. This in turn results in conformational differences among subunits and overall asymmetry of the motor ring as it functions. To date, a large amount of structural information has been gathered for different AAA+ motors, but even for the most characterized of them only a few structural states are known and the full mechanistic cycle cannot be yet reconstructed. Therefore, the first part of this work will provide a broad overview of what arrangements of AAA+ subunits have been structurally observed focusing on diversity of ATPase oligomeric ensembles and heterogeneity within the ensembles. The second part of this review will concentrate on methods that assess structural and functional heterogeneity among subunits of AAA+ motors, thus bringing us closer to understanding the mechanism of these fascinating molecular motors.
FtsH-related AAA proteases are conserved membrane-anchored, ATP-dependent molecular machines, which mediate the processing and turnover of soluble and membrane-embedded proteins in eubacteria, mitochondria, and chloroplasts. Homo- and hetero-oligomeric proteolytic complexes exist, which are composed of homologous subunits harboring an ATPase domain of the AAA family and an H41 metallopeptidase domain. Mutations in subunits of mitochondrial m-AAA proteases have been associated with different neurodegenerative disorders in human, raising questions on the functional differences between homo- and hetero-oligomeric AAA proteases. Here, we have analyzed the hetero-oligomeric yeast m-AAA protease composed of homologous Yta10 and Yta12 subunits. We combined genetic and structural approaches to define the molecular determinants for oligomer assembly and to assess functional similarities between Yta10 and Yta12. We demonstrate that replacement of only two amino acid residues within the metallopeptidase domain of Yta12 allows its assembly into homo-oligomeric complexes. To provide a molecular explanation, we determined the 12 Å resolution structure of the intact yeast m-AAA protease with its transmembrane domains by electron cryomicroscopy (cryo-EM) and atomic structure fitting. The full-length m-AAA protease has a bipartite structure and is a hexamer in solution. We found that residues in Yta12, which facilitate homo-oligomerization when mutated, are located at the interface between neighboring protomers in the hexamer ring. Notably, the transmembrane and intermembrane space domains are separated from the main body, creating a passage on the matrix side, which is wide enough to accommodate unfolded but not folded polypeptides. These results suggest a mechanism regarding how proteins are recognized and degraded by m-AAA proteases.
Baltimore, Philadelphia, and Washington, DC are geographically proximate cities with high HIV prevalence, including among black men who have sex with men (BMSM). Using data collected among BMSM in CDC's National HIV Behavioral Surveillance project, we compared socio-demographic characteristics, HIV risk behaviors, and service utilization to explore similarities and differences that could inform local and regional HIV intervention approaches. BMSM were recruited through venue time location sampling, June-December, 2011. Participants completed identical socio-behavioral surveys and voluntary HIV testing. Analyses were conducted among the full sample and those aged 18-24. Participants included 159 (DC), 364 (Baltimore), and 331 (Philadelphia) eligible BMSM. HIV prevalence was 23.1% (DC), 48.0% (Baltimore), 14.6% (Philadelphia) with 30.6%, 69.0%, 33.3% unrecognized HIV infection, respectively. Among BMSM 18-24, HIV prevalence was 11.1% (DC), 38.9% (Baltimore), 9.6% (Philadelphia) with unrecognized HIV infection 0.0%, 73.8%, 60.0% respectively. Compared with the other 2 cities, Baltimore participants were less likely to identify as gay/homosexual; more likely to report unemployment, incarceration, homelessness, sex exchange; and least likely to use the internet for partners. DC participants were more likely to have a college degree and employment. Philadelphia participants were more likely to report gay/homosexual identity, receptive condomless anal sex, having only main partners, and bars/clubs as partner meeting places. Sexually transmitted disease testing was universally low. Analyses showed especially high HIV prevalence among BMSM in Baltimore including among young BMSM. Socio-demographic characteristics and HIV infection correlates differed across cities but unrecognized HIV infection and unknown partner status were universally high.
The crystal structure of a conserved hypothetical protein from L. major, Pfam sequence family PF04543, structural genomics target ID Lmaj006129AAA, has been determined at a resolution of 1.6 Å. The gene product of structural genomics target Lmaj006129 from Leishmania major codes for a 164-residue protein of unknown function. When SeMet expression of the full-length gene product failed, several truncation variants were created with the aid of Ginzu, a domain-prediction method. 11 truncations were selected for expression, purification and crystallization based upon secondary-structure elements and disorder. The structure of one of these variants, Lmaj006129AAH, was solved by multiple-wavelength anomalous diffraction (MAD)more using ELVES, an automatic protein crystal structure-determination system. This model was then successfully used as a molecular-replacement probe for the parent full-length target, Lmaj006129AAA. The final structure of Lmaj006129AAA was refined to an R value of 0.185 (Rsub free = 0.229) at 1.60 Å resolution. Structure and sequence comparisons based on Lmaj006129AAA suggest that proteins belonging to Pfam sequence families PF04543 and PF01878 may share a common ligand-binding motif. less 2ff7e9595c
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