Losing identity: structural diversity of transposable elements belonging to different classes in the genome of Anopheles gambiae

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Light-front zero-mode contribution to the Ward Identity

In a covariant gauge we implicitly assume that the Green's function propagates information from one point of the space-time to another, so that the Green's function is responsible for the dynamics of the relativistic particle. In the light front form one would naively expect, that this feature would be preserved. In this manner, the fermionic field propagator can be split into a propagating piece and a non-propagating (contact) term. Since the latter (contact) one does not propagate information; and therefore, supposedly can be discarded with no harm to the field dynamics we wanted to know what would be the impact of dropping it off. To do that, we investigated its role in the Ward identity in the light front. Here we use the terminology Ward identity to identify the limiting case of photon's zero momentum transfer in the vertex from the more general Ward-Takahashi identity with nonzero momentum transfer.

UMP kinase from Mycobacterium tuberculosis: Mode of action and allosteric interactions, and their likely role in pyrimidine metabolism regulation

The pyrH-encoded uridine 5′-monophosphate kinase (UMPK) is involved in both de novo and salvage synthesis of DNA and RNA precursors. Here we describe Mycobacterium tuberculosis UMPK (MtUMPK) cloning and expression in Escherichia coli. N-terminal amino acid sequencing and electrospray ionization mass spectrometry analyses confirmed the identity of homogeneous MtUMPK. MtUMPK catalyzed the phosphorylation of UMP to UDP, using ATP-Mg 2+ as phosphate donor. Size exclusion chromatography showed that the protein is a homotetramer. Kinetic studies revealed that MtUMPK exhibits cooperative kinetics towards ATP and undergoes allosteric regulation. GTP and UTP are, respectively, positive and negative effectors, maintaining the balance of purine versus pyrimidine synthesis. Initial velocity studies and substrate(s) binding measured by isothermal titration calorimetry suggested that catalysis proceeds by a sequential ordered mechanism, in which ATP binds first followed by UMP binding, and release of products is random. As MtUMPK does not resemble its eukaryotic counterparts, specific inhibitors could be designed to be tested as antitubercular agents. © 2010 Elsevier Inc. All rights reserved.

B chromosomes in species of the genus Prochilodus (Characiformes, Prochilodontidae): morphological identity and dispersion

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)