Propuesta de Mecanismos de Verificación de Integridad de Plataformas Móviles de Computación basados en Entornos Seguros de Ejecución

Las prestaciones y características de los dispositivos móviles actuales los sitúa a un nivel similar a los ordenadores de escritorio tradicionales en cuanto a funcionalidad y posibilidades de uso, añadiendo además la movilidad y la sensación de pertenencia al usuario que se deriva de ésta. Estas cualidades convierten a las plataformas móviles de computación en verdaderos ordenadores personales, y cada día es más popular su utilización en ámbitos distintos del ocio y las comunicaciones propiamente dichas, pasando a convertirse en herramientas de apoyo a la productividad también en el entorno profesional y corporativo. La utilización del dispositivo móvil como parte de una infraestructura de telecomunicaciones da lugar a nuevas expresiones de problemas clásicos de gestión y seguridad. Para tratar de abordarlos con la flexibilidad y la escalabilidad necesarias se plantean alternativas novedosas que parten de enfoques originales a estos problemas, como las ideas y conceptos que se engloban en la filosofía del Control de Acceso a la Red (Network Access Control, o NAC). La mayoría de los planteamientos de NAC se basan, en el ámbito de la seguridad, en comprobar ciertas características del dispositivo móvil para tratar de determinar hasta qué punto puede éste suponer una amenaza para los recursos de la red u otros usuarios de la misma. Obtener esta información de forma fiable resulta extremadamente difícil si se caracteriza el dispositivo mediante un modelo de caja blanca, muy adecuado dada la apertura propia de los sistemas operativos móviles actuales, muy diferentes de los de antaño, y la ausencia de un marco de seguridad efectivo en ellos. Este trabajo explora el Estado de la Técnica en este ámbito de investigación y plantea diferentes propuestas orientadas a cubrir las deficiencias de las soluciones propuestas hasta el momento y a satisfacer los estrictos requisitos de seguridad que se derivan de la aplicación del modelo de caja blanca, materializándose en última instancia en la definición de un mecanismo de evaluación de características arbitrarias de un cierto dispositivo móvil basado en Entornos Seguros de Ejecución (Trusted Execution Environments, o TEEs) con elevadas garantías de seguridad compatible con los planteamientos actuales de NAC. ABSTRACT The performance and features of today’s mobile devices make them able to compete with traditional desktop computers in terms of functionality and possible usages. In addition to this, they sport mobility and the stronger sense of ownership that derives from it. These attributes change mobile computation platforms into truly personal computers, allowing them to be used not only for leisure or as mere communications devices, but also as supports of productivity in professional and corporative environments. The utilization of mobile devices as part of a telecommunications infrastructure brings new expressions of classic management and security problems with it. In order to tackle them with appropriate flexibility and scalability, new alternatives are proposed based on original approaches to these problems, such as the concepts and ideas behind the philosophy of Network Access Control (NAC). The vast majority of NAC proposals are based, security-wise, on checking certain mobile device’s properties in order to evaluate how probable it is for it to become a threat for network resources or even other users of the infrastructure. Obtaining this information in a reliable and trustworthy way is extremely difficult if the device is characterized using a white-box model, which is the most appropriate if the openness of today’s mobile operating systems, very different from former ones, and the absence of an effective security framework are taken into account. This work explores the State of the Art related with the aforementioned field of research and presents different proposals targeted to overcome the deficiencies of current solutions and satisfy the strict security requirements derived from the application of the white box model. These proposals are ultimately materialized in the definition of a high-security evaluation procedure of arbitrary properties of a given mobile device based on Trusted Execution Environments (TEEs) which is compatible with modern NAC approaches.

OSIRIS – The scientific camera system onboard Rosetta

The Optical, Spectroscopic, and Infrared Remote Imaging System OSIRIS is the scientific camera system onboard the Rosetta spacecraft (Figure 1). The advanced high performance imaging system will be pivotal for the success of the Rosetta mission. OSIRIS will detect 67P/Churyumov-Gerasimenko from a distance of more than 106 km, characterise the comet shape and volume, its rotational state and find a suitable landing spot for Philae, the Rosetta lander. OSIRIS will observe the nucleus, its activity and surroundings down to a scale of ~2 cm px−1. The observations will begin well before the onset of cometary activity and will extend over months until the comet reaches perihelion. During the rendezvous episode of the Rosetta mission, OSIRIS will provide key information about the nature of cometary nuclei and reveal the physics of cometary activity that leads to the gas and dust coma. OSIRIS comprises a high resolution Narrow Angle Camera (NAC) unit and a Wide Angle Camera (WAC) unit accompanied by three electronics boxes. The NAC is designed to obtain high resolution images of the surface of comet 7P/Churyumov-Gerasimenko through 12 discrete filters over the wavelength range 250–1000 nm at an angular resolution of 18.6 μrad px−1. The WAC is optimised to provide images of the near-nucleus environment in 14 discrete filters at an angular resolution of 101 μrad px−1. The two units use identical shutter, filter wheel, front door, and detector systems. They are operated by a common Data Processing Unit. The OSIRIS instrument has a total mass of 35 kg and is provided by institutes from six European countries

Observations of Comet 9P/Tempel 1 around the Deep Impact event by the OSIRIS cameras onboard Rosetta

The OSIRIS cameras on the Rosetta spacecraft observed Comet 9P/Tempel 1 from 5 days before to 10 days after it was hit by the Deep Impact projectile. The Narrow Angle Camera (NAC) monitored the cometary dust in 5 different filters. The Wide Angle Camera (WAC) observed through filters sensitive to emissions from OH, CN, Na, and OI together with the associated continuum. Before and after the impact the comet showed regular variations in intensity. The period of the brightness changes is consistent with the rotation period of Tempel 1. The overall brightness of Tempel 1 decreased by about 10% during the OSIRIS observations. The analysis of the impact ejecta shows that no new permanent coma structures were created by the impact. Most of the material moved with View the MathML source∼200ms−1. Much of it left the comet in the form of icy grains which sublimated and fragmented within the first hour after the impact. The light curve of the comet after the impact and the amount of material leaving the comet (View the MathML source4.5–9×106kg of water ice and a presumably larger amount of dust) suggest that the impact ejecta were quickly accelerated by collisions with gas molecules. Therefore, the motion of the bulk of the ejecta cannot be described by ballistic trajectories, and the validity of determinations of the density and tensile strength of the nucleus of Tempel 1 with models using ballistic ejection of particles is uncertain.

A general mechanism for regulation of access to the translocon: Competition for a membrane attachment site on ribosomes

For proteins to enter the secretory pathway, the membrane attachment site (M-site) on ribosomes must bind cotranslationally to the Sec61 complex present in the endoplasmic reticulum membrane. The signal recognition particle (SRP) and its receptor (SR) are required for targeting, and the nascent polypeptide associated complex (NAC) prevents inappropriate targeting of nonsecretory nascent chains. In the absence of NAC, any ribosome, regardless of the polypeptide being synthesized, binds to the endoplasmic reticulum membrane, and even nonsecretory proteins are translocated across the endoplasmic reticulum membrane. By occupying the M-site, NAC prevents all ribosome binding unless a signal peptide and SRP are present. The mechanism by which SRP overcomes the NAC block is unknown. We show that signal peptide-bound SRP occupies the M-site and therefore keeps it free of NAC. To expose the M-site and permit ribosome binding, SR can pull SRP away from the M-site without prior release of SRP from the signal peptide.

Signal Recognition Particle-dependent Targeting of Ribosomes to the Rough Endoplasmic Reticulum in the Absence and Presence of the Nascent Polypeptide-associated Complex

Proteins with RER-specific signal sequences are cotranslationally translocated across the rough endoplasmic reticulum through a proteinaceous channel composed of oligomers of the Sec61 complex. The Sec61 complex also binds ribosomes with high affinity. The dual function of the Sec61 complex necessitates a mechanism to prevent signal sequence-independent binding of ribosomes to the translocation channel. We have examined the hypothesis that the signal recognition particle (SRP) and the nascent polypeptide-associated complex (NAC), respectively, act as positive and negative regulatory factors to mediate the signal sequence-specific attachment of the ribosome-nascent chain complex (RNC) to the translocation channel. Here, SRP-independent translocation of a nascent secretory polypeptide was shown to occur in the presence of endogenous wheat germ or rabbit reticulocyte NAC. Furthermore, SRP markedly enhanced RNC binding to the translocation channel irrespective of the presence of NAC. Binding of RNCs, but not SRP-RNCs, to the Sec61 complex is competitively inhibited by 80S ribosomes. Thus, the SRP-dependent targeting pathway provides a mechanism for delivery of RNCs to the translocation channel that is not inhibited by the nonselective interaction between the ribosome and the Sec61 complex.

Nascent Polypeptide–associated Complex Stimulates Protein Import into Yeast Mitochondria

To identify yeast cytosolic proteins that mediate targeting of precursor proteins to mitochondria, we developed an in vitro import system consisting of purified yeast mitochondria and a radiolabeled mitochondrial precursor protein whose C terminus was still attached to the ribosome. In this system, the N terminus of the nascent chain was translocated across both mitochondrial membranes, generating a translocation intermediate spanning both membranes. The nascent chain could then be completely chased into the mitochondrial matrix after release from the ribosome. Generation of this import intermediate was dependent on a mitochondrial membrane potential, mitochondrial surface proteins, and was stimulated by proteins that could be released from the ribosomes by high salt. The major salt-released stimulatory factor was yeast nascent polypeptide–associated complex (NAC). Purified NAC fully restored import of salt-washed ribosome-bound nascent chains by enhancing productive binding of the chains to mitochondria. We propose that ribosome-associated NAC facilitates recognition of nascent precursor chains by the mitochondrial import machinery.

Essential role for complex N-glycans in forming an organized layer of bronchial epithelium.

Mice lacking the complex subset of N-glycans due to inactivation of the Mgat1 gene die at mid-gestation, making it difficult to identify specific biological functions for this class of cell surface carbohydrates. To circumvent this embryonic lethality and to uncover tissue-specific functions for complex N-glycans, WW6 embryonic stem cells with inactivated Mgat1 alleles were tracked in chimeric embryos. The Mgat1 gene encodes N-acetylglucosaminyltransferase I (Glc-NAc-TI; EC 2.4.1.101), the transferase that initiates the synthesis of complex N-glycans. WW6 cells carry an inert beta-globin transgene that allows their identification in chimeras by DNA-DNA in situ hybridization. Independent Mgat1-/- and Mgat1+/- mutant WW6 isolates contributed like parent WW6 cells to the tissues of embryonic day (E) 10.5 to E16.5 chimeras. However, a cell type-specific difference was observed in lung. Homozygous null Mgat1-/- WW6 cells did not contribute to the epithelial layer in more than 99% bronchi. This deficiency was corrected by transfection of a Mgat1 transgene. Interestingly, heterozygous Mgat1+/- WW6 cells were also deficient in populating the layer of bronchial epithelium. Furthermore, examination of lung bud in E9.5 Mgat1-/- mutant embryos showed complete absence of an organized epithelial cell layer in the bronchus. Thus, complex N-glycans are required to form a morphologically recognizable bronchial epithelium, revealing an in vivo, cell type-specific function for this class of N-glycans.