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Prokaryotic Organisms (prokaryotic + organism)
Selected AbstractsFunctional characterization of the evolutionarily divergent fern plastocyaninFEBS JOURNAL, Issue 16 2004José A. Navarro Plastocyanin (Pc) is a soluble copper protein that transfers electrons from cytochrome b6f to photosystem I (PSI), two protein complexes that are localized in the thylakoid membranes in chloroplasts. The surface electrostatic potential distribution of Pc plays a key role in complex formation with the membrane-bound partners. It is practically identical for Pcs from plants and green algae, but is quite different for Pc from ferns. Here we report on a laser flash kinetic analysis of PSI reduction by Pc from various eukaryotic and prokaryotic organisms. The reaction of fern Pc with fern PSI fits a two-step kinetic model, consisting of complex formation and electron transfer, whereas other plant systems exhibit a mechanism that requires an additional intracomplex rearrangement step. The fern Pc interacts inefficiently with spinach PSI, showing no detectable complex formation. This can be explained by assuming that the unusual surface charge distribution of fern Pc impairs the interaction. Fern PSI behaves in a similar way as spinach PSI in reaction with other Pcs. The reactivity of fern Pc towards several soluble c -type cytochromes, including cytochrome f, has been analysed by flavin-photosensitized laser flash photolysis, demonstrating that the specific surface motifs for the interaction with cytochrome f are conserved in fern Pc. [source] Click Chemistry-Led Advances in High Content Functional ProteomicsMOLECULAR INFORMATICS, Issue 11-12 2007Abstract The availability of complete genome sequences for numerous eukaryotic and prokaryotic organisms has inspired the advent of new methods to functionally characterize proteins on a global scale. Chemical approaches, in particular, have emerged as a powerful way to investigate the proteome, providing small-molecule probes that report on protein activity and Post-Translational Modification (PTM) state directly in complex biological samples. Many of the key advances made in chemical proteomics can be attributed to the development of efficient bio-orthogonal reactions such as the copper (I)-catalyzed Huisgen's azide,alkyne cycloaddition, a reaction commonly known as "Click Chemistry" (CC). The generation of "clickable" proteomics probes has removed the requirement for bulky reporter tags, thereby allowing access to more biologically relevant systems such as live cells or animals. The versatility of CC has also allowed for greater experimental efficiency, as different reporter tags (i.e., a fluorophore for detection or biotin for enrichment) can be appended to a single probe. Such advances have enabled researchers to identify protein activities dysregulated in disease states, assess the selectivity of enzyme inhibitors in vivo, and inventory specific PTMs on a proteome-wide scale. [source] A novel bacterial signalling system with a combination of a Ser/Thr kinase cascade and a His/Asp two-component systemMOLECULAR MICROBIOLOGY, Issue 2 2005Renate Lux Summary Prokaryotes and eukaryotes have long been thought to use very different types of kinases (the His kinases of the ,bacterial' two-component systems versus the ,eukaryotic' Ser/Thr/Tyr kinases) to carry out signal transduction. This paradigm no longer holds true, because both systems are now found together in an increasing number of prokaryotic organisms and ,two-component' His kinase are present in eukaryotes. Pioneering work on bacterial protein serine threonine kinases (PSTKs) has been performed in Myxococcus xanthus, a soil bacterium with a complex life cycle that possesses orthologues of signalling-related kinases ,typical' of both the prokaryotic and the eukaryotic kingdoms. In the work reported in this volume of Molecular Microbiology, Nariya and Inouye describe a PSTK cascade that modulates the biochemical activity of MrpC, a CRP-like transcriptional regulator for essential developmental signalling pathways in M. xanthus whose transcription is under the control of a two-component system. This is the first report of both a functional PSTK cascade in bacteria and the use of both PSTK and two-component systems to control a single complex bacterial signalling event. [source] The Campylobacter jejuni stringent response controls specific stress survival and virulence-associated phenotypesMOLECULAR MICROBIOLOGY, Issue 1 2005Erin C. Gaynor Summary Campylobacter jejuni is a highly prevalent food-borne pathogen that causes diarrhoeal disease in humans. A natural zoonotic, it must overcome significant stresses both in vivo and during transmission despite the absence of several traditional stress response genes. Although relatively little is understood about its mechanisms of pathogenesis, its ability to interact with and invade human intestinal epithelial cells closely correlates with virulence. A C. jejuni microarray-based screen revealed that several known virulence genes and several uncharacterized genes, including spoT, were rapidly upregulated during infection of human epithelial cells. spoT and its homologue relA have been shown in other bacteria to regulate the stringent response, an important stress response that to date had not been demonstrated for C. jejuni or any other epsilon-proteobacteria. We have found that C. jejuni mounts a stringent response that is regulated by spoT. Detailed analyses of a C. jejuni,spoT mutant revealed that the stringent response is required for several specific stress, transmission and antibiotic resistance-related phenotypes. These include stationary phase survival, growth and survival under low CO2/high O2 conditions, and rifampicin resistance. A secondary suppressor strain that specifically rescues the low CO2 growth defect of the ,spoT mutant was also isolated. The stringent response additionally proved to be required for the virulence-related phenotypes of adherence, invasion, and intracellular survival in two human epithelial cell culture models of infection; spoT is the first C. jejuni gene shown to participate in longer term survival in epithelial cells. Microarray analyses comparing wild-type to the ,spoT mutant also revealed a strong correlation between gene expression profiles and phenotype differences observed. Together, these data demonstrate a critical role for the C. jejuni stringent response in multiple aspects of C. jejuni biology and pathogenesis and, further, may lend novel insight into unexplored features of the stringent response in other prokaryotic organisms. [source] Calcium signalling in bacteriaMOLECULAR MICROBIOLOGY, Issue 2 2004Delfina C. Dominguez Summary Whereas the importance of calcium as a cell regulator is well established in eukaryotes, the role of calcium in prokaryotes is still elusive. Over the past few years, there has been an increased interest in the role of calcium in bacteria. It has been demonstrated that as in eukaryotic organisms, the intracellular calcium concentration in prokaryotes is tightly regulated ranging from 100 to 300 nM. It has been found that calcium ions are involved in the maintenance of cell structure, motility, transport and cell differentiation processes such as sporulation, heterocyst formation and fruiting body development. In addition, a number of calcium-binding proteins have been isolated in several prokaryotic organisms. The characterization of these proteins and the identification of other factors suggest the possibility that calcium signal transduction exists in bacteria. This review presents recent developments of calcium in bacteria as it relates to signal transduction. [source] A dual infection by infectious cuticular epithelial necrosis virus and a Chlamydia -like organism in cultured Litopenaeus vannamei (Boone) in EcuadorAQUACULTURE RESEARCH, Issue 11 2001R Jimenez During 1996, microscopic examinations of post larvae and juveniles of moribund Litopenaeus vannamei showed multifocal necrosis in the cuticular epithelial tissues. In addition to these severe degenerative alterations in the epithelial cells typical of infectious cuticular epithelial necrosis virus (ICENV), columnar cells of the epithelium displayed small round intracytoplasmic inclusions in the necrotic tissue. Examination by electron microscopy of affected tissues demonstrated prokaryotic organisms in the cytoplasm of epithelial cells delineated by a distinct cytoplasmic vesicle; the prokaryotic organisms were morphologically similar to the genus Chlamydia. The necrotic tissue also showed the presence of particles of ICENV; the double infection by two different organisms in cuticular epithelial cells has not been reported previously. Two distinct stages in the intracellular development of a Chlamydia -like organism were recognized: (1) pleomorphic elementary bodies (EBs) that were spherical to oval were often observed in the process of division or in forming a common chain of three cells, the cells were surrounded by a rigid cell envelope and the presence of a cap or plaque hexagonally arrayed; (2) the reticular bodies (RBs) were forms often in the process of division. These cells had an electron-dense cytoplasm and contained a loose network of nuclear fibrils and a more fragile cell envelope. Regardless of the development stages of the Chlamydia -like organism within the cytoplasmic vesicles, ICENV particles were observed, either dispersed or in clusters, surrounded or inside the vesicles. The potential adverse impact of this dual infection on shrimp culture should be considered, especially in high-density operations. [source] Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimuriumACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2009Hugh P. Morgan In prokaryotic organisms, cold shock triggers the production of a small highly conserved family of cold-shock proteins (CSPs). CSPs have been well studied structurally and functionally in Escherichia coli and Bacillus subtilis, but Salmonella typhimurium CSPs remain relatively uncharacterized. In S. typhimurium, six homologous CSPs have been identified: StCspA,E and StCspH. The crystal structure of cold-shock protein E from S. typhimurium (StCspE) has been determined at 1.1,Å resolution and has an R factor of 0.203 after refinement. The three-dimensional structure is similar to those of previously determined CSPs and is composed of five antiparallel ,-strands forming a classic OB fold/five-stranded ,-barrel. This first structure of a CSP from S. typhimurium provides new insight into the cold-shock response of this bacterium. [source] | ||||||||||