The Experts below are selected from a list of 16680 Experts worldwide ranked by ideXlab platform
J Laskar - One of the best experts on this subject based on the ideXlab platform.
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a high power cmos switch using a novel adaptive voltage swing distribution method in multistack fets
IEEE Transactions on Microwave Theory and Techniques, 2008Co-Authors: J LaskarAbstract:A high-power CMOS switch using a novel adaptive voltage swing distribution method in a multistack field-effect transistor (FET) scheme is proposed. The proposed adaptive voltage swing distribution method in multistack FETs is very effective in Preventing unwanted channel formation with low control voltage supply in OFF-state FETs. This, in turn, increases power-handling capability when a large-signal voltage swing is applied. In the proposed CMOS switch, the behavior of the voltage swing in OFF-state multistack FETs shows a difference with respect to the level of input voltage swing. The characteristics of voltage swing distribution and leakage channel formation in the CMOS switch is fully analyzed with incorporation of the novel adaptive voltage swing distribution method into a three-stacked nMOS Rx switch in a standard 0.18-mum triple-well CMOS process. In addition, linearity of the proposed technique is verified through the measurement data of the single-pole double-throw switches that employ the proposed technique in the Rx switch. Two different types of configurations are implemented and characterized at the Rx switches, which consist of four-stacked nMOS devices, to demonstrate the method of minimizing voltage stress issues on one of the multistacked FETs. Layout consideration was also taken to Prevent Interference between leakage signals at the substrate. The measured performance of the proposed design shows an input 0.3-dB compression point of 33.5 dBm at 1.9 GHz. To the best of our knowledge, this is the highest power-handling capability of a CMOS switch in a standard CMOS process ever reported. The insertion losses of the Tx and Rx switches are 1.6 and 1.9 dB, respectively, at 1.9 GHz. The isolation of the Tx and Rx switches is around 20 and 30 dB, respectively, at 1.9 GHz.
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a high power cmos switch using a novel adaptive voltage swing distribution method in multistack fets
IEEE Transactions on Microwave Theory and Techniques, 2008Co-Authors: Minsik Ahn, Changho Lee, Byungsung Kim, J LaskarAbstract:A high-power CMOS switch using a novel adaptive voltage swing distribution method in a multistack field-effect transistor (FET) scheme is proposed. The proposed adaptive voltage swing distribution method in multistack FETs is very effective in Preventing unwanted channel formation with low control voltage supply in OFF-state FETs. This, in turn, increases power-handling capability when a large-signal voltage swing is applied. In the proposed CMOS switch, the behavior of the voltage swing in OFF-state multistack FETs shows a difference with respect to the level of input voltage swing. The characteristics of voltage swing distribution and leakage channel formation in the CMOS switch is fully analyzed with incorporation of the novel adaptive voltage swing distribution method into a three-stacked nMOS Rx switch in a standard 0.18-mum triple-well CMOS process. In addition, linearity of the proposed technique is verified through the measurement data of the single-pole double-throw switches that employ the proposed technique in the Rx switch. Two different types of configurations are implemented and characterized at the Rx switches, which consist of four-stacked nMOS devices, to demonstrate the method of minimizing voltage stress issues on one of the multistacked FETs. Layout consideration was also taken to Prevent Interference between leakage signals at the substrate. The measured performance of the proposed design shows an input 0.3-dB compression point of 33.5 dBm at 1.9 GHz. To the best of our knowledge, this is the highest power-handling capability of a CMOS switch in a standard CMOS process ever reported. The insertion losses of the Tx and Rx switches are 1.6 and 1.9 dB, respectively, at 1.9 GHz. The isolation of the Tx and Rx switches is around 20 and 30 dB, respectively, at 1.9 GHz.
Bart L Staker - One of the best experts on this subject based on the ideXlab platform.
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structural insight into how bacteria Prevent Interference between multiple divergent type iv secretion systems
Mbio, 2015Co-Authors: Joseph J Gillespie, Isabelle Q Phan, Holger Scheib, Sandhya Subramanian, Thomas E Edwards, Stephanie S Lehman, Hanna Piitulainen, Sayeedur M Rahman, Kristen E Rennollbankert, Bart L StakerAbstract:ABSTRACT Prokaryotes use type IV secretion systems (T4SSs) to translocate substrates (e.g., nucleoprotein, DNA, and protein) and/or elaborate surface structures (i.e., pili or adhesins). Bacterial genomes may encode multiple T4SSs, e.g., there are three functionally divergent T4SSs in some Bartonella species ( vir , vbh , and trw ). In a unique case, most rickettsial species encode a T4SS ( rvh ) enriched with gene duplication. Within single genomes, the evolutionary and functional implications of cross-system interchangeability of analogous T4SS protein components remains poorly understood. To lend insight into cross-system interchangeability, we analyzed the VirB8 family of T4SS channel proteins. Crystal structures of three VirB8 and two TrwG Bartonella proteins revealed highly conserved C-terminal periplasmic domain folds and dimerization interfaces, despite tremendous sequence divergence. This implies remarkable structural constraints for VirB8 components in the assembly of a functional T4SS. VirB8/TrwG heterodimers, determined via bacterial two-hybrid assays and molecular modeling, indicate that differential expression of trw and vir systems is the likely barrier to VirB8-TrwG interchangeability. We also determined the crystal structure of Rickettsia typhi RvhB8-II and modeled its coexpressed divergent paralog RvhB8-I. Remarkably, while RvhB8-I dimerizes and is structurally similar to other VirB8 proteins, the RvhB8-II dimer interface deviates substantially from other VirB8 structures, potentially Preventing RvhB8-I/RvhB8-II heterodimerization. For the rvh T4SS, the evolution of divergent VirB8 paralogs implies a functional diversification that is unknown in other T4SSs. Collectively, our data identify two different constraints (spatiotemporal for Bartonella trw and vir T4SSs and structural for rvh T4SSs) that mediate the functionality of multiple divergent T4SSs within a single bacterium. IMPORTANCE Assembly of multiprotein complexes at the right time and at the right cellular location is a fundamentally important task for any organism. In this respect, bacteria that express multiple analogous type IV secretion systems (T4SSs), each composed of around 12 different components, face an overwhelming complexity. Our work here presents the first structural investigation on factors regulating the maintenance of multiple T4SSs within a single bacterium. The structural data imply that the T4SS-expressing bacteria rely on two strategies to Prevent cross-system interchangeability: (i) tight temporal regulation of expression or (ii) rapid diversification of the T4SS components. T4SSs are ideal drug targets provided that no analogous counterparts are known from eukaryotes. Drugs targeting the barriers to cross-system interchangeability (i.e., regulators) could dysregulate the structural and functional independence of discrete systems, potentially creating Interference that Prevents their efficient coordination throughout bacterial infection.
Claire Moore - One of the best experts on this subject based on the ideXlab platform.
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dismantling promoter driven rna polymerase ii transcription complexes in vitro by the termination factor rat1
Journal of Biological Chemistry, 2013Co-Authors: Erika L Pearson, Claire MooreAbstract:Abstract Proper RNA Polymerase II (Pol II) transcription termination is essential to generate stable transcripts, to Prevent Interference at downstream loci, and to recycle Pol II back to the promoter (1-3). As such, termination is an intricately controlled process that is tightly regulated by a variety of different cis- and trans-acting factors (4, 5). Although many eukaryotic termination factors have been identified to date, the details of the precise molecular mechanisms governing termination remain to be elucidated. To tease apart these details, we have devised an in vitro transcription system to assay for specific Pol II termination. We show for the first time that the exonucleolytic Rat1/Rai1 complex can elicit release of stalled Pol II in vitro and can do so in the absence of other factors. We also find that Rtt103, which interacts with the Pol II C-terminal domain (CTD) and with Rat1, can rescue termination activity of an exonucleolytically deficient Rat1 mutant. In light of our findings, we posit a model whereby functional nucleolytic activity is not the feature of Rat1 that ultimately promotes termination. Degradation of the nascent transcript allows Rat1 to pursue Pol II in a guided fashion and to arrive at the site of RNA exit from Pol II. Upon this arrival, however, it is perhaps the specific and direct contact between Rat1 and Pol II that transmits the signal to terminate transcription.
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dismantling promoter driven rna polymerase ii transcription complexes in vitro by the termination factor rat1
Journal of Biological Chemistry, 2013Co-Authors: Erika L Pearson, Claire MooreAbstract:Proper RNA polymerase II (Pol II) transcription termination is essential to generate stable transcripts, to Prevent Interference at downstream loci, and to recycle Pol II back to the promoter (1-3). As such, termination is an intricately controlled process that is tightly regulated by a variety of different cis- and trans-acting factors (4, 5). Although many eukaryotic termination factors have been identified to date, the details of the precise molecular mechanisms governing termination remain to be elucidated. We devised an in vitro transcription system to study specific Pol II termination. We show for the first time that the exonucleolytic Rat1·Rai1 complex can elicit the release of stalled Pol II in vitro and can do so in the absence of other factors. We also find that Rtt103, which interacts with the Pol II C-terminal domain (CTD) and with Rat1, can rescue termination activity of an exonucleolytically deficient Rat1 mutant. In light of our findings, we posit a model whereby functional nucleolytic activity is not the feature of Rat1 that ultimately promotes termination. Degradation of the nascent transcript allows Rat1 to pursue Pol II in a guided fashion and arrive at the site of RNA exit from Pol II. Upon this arrival, however, it is perhaps the specific and direct contact between Rat1 and Pol II that transmits the signal to terminate transcription.
Joseph J Gillespie - One of the best experts on this subject based on the ideXlab platform.
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structural insight into how bacteria Prevent Interference between multiple divergent type iv secretion systems
Mbio, 2015Co-Authors: Joseph J Gillespie, Isabelle Q Phan, Holger Scheib, Sandhya Subramanian, Thomas E Edwards, Stephanie S Lehman, Hanna Piitulainen, Sayeedur M Rahman, Kristen E Rennollbankert, Bart L StakerAbstract:ABSTRACT Prokaryotes use type IV secretion systems (T4SSs) to translocate substrates (e.g., nucleoprotein, DNA, and protein) and/or elaborate surface structures (i.e., pili or adhesins). Bacterial genomes may encode multiple T4SSs, e.g., there are three functionally divergent T4SSs in some Bartonella species ( vir , vbh , and trw ). In a unique case, most rickettsial species encode a T4SS ( rvh ) enriched with gene duplication. Within single genomes, the evolutionary and functional implications of cross-system interchangeability of analogous T4SS protein components remains poorly understood. To lend insight into cross-system interchangeability, we analyzed the VirB8 family of T4SS channel proteins. Crystal structures of three VirB8 and two TrwG Bartonella proteins revealed highly conserved C-terminal periplasmic domain folds and dimerization interfaces, despite tremendous sequence divergence. This implies remarkable structural constraints for VirB8 components in the assembly of a functional T4SS. VirB8/TrwG heterodimers, determined via bacterial two-hybrid assays and molecular modeling, indicate that differential expression of trw and vir systems is the likely barrier to VirB8-TrwG interchangeability. We also determined the crystal structure of Rickettsia typhi RvhB8-II and modeled its coexpressed divergent paralog RvhB8-I. Remarkably, while RvhB8-I dimerizes and is structurally similar to other VirB8 proteins, the RvhB8-II dimer interface deviates substantially from other VirB8 structures, potentially Preventing RvhB8-I/RvhB8-II heterodimerization. For the rvh T4SS, the evolution of divergent VirB8 paralogs implies a functional diversification that is unknown in other T4SSs. Collectively, our data identify two different constraints (spatiotemporal for Bartonella trw and vir T4SSs and structural for rvh T4SSs) that mediate the functionality of multiple divergent T4SSs within a single bacterium. IMPORTANCE Assembly of multiprotein complexes at the right time and at the right cellular location is a fundamentally important task for any organism. In this respect, bacteria that express multiple analogous type IV secretion systems (T4SSs), each composed of around 12 different components, face an overwhelming complexity. Our work here presents the first structural investigation on factors regulating the maintenance of multiple T4SSs within a single bacterium. The structural data imply that the T4SS-expressing bacteria rely on two strategies to Prevent cross-system interchangeability: (i) tight temporal regulation of expression or (ii) rapid diversification of the T4SS components. T4SSs are ideal drug targets provided that no analogous counterparts are known from eukaryotes. Drugs targeting the barriers to cross-system interchangeability (i.e., regulators) could dysregulate the structural and functional independence of discrete systems, potentially creating Interference that Prevents their efficient coordination throughout bacterial infection.
Erika L Pearson - One of the best experts on this subject based on the ideXlab platform.
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dismantling promoter driven rna polymerase ii transcription complexes in vitro by the termination factor rat1
Journal of Biological Chemistry, 2013Co-Authors: Erika L Pearson, Claire MooreAbstract:Abstract Proper RNA Polymerase II (Pol II) transcription termination is essential to generate stable transcripts, to Prevent Interference at downstream loci, and to recycle Pol II back to the promoter (1-3). As such, termination is an intricately controlled process that is tightly regulated by a variety of different cis- and trans-acting factors (4, 5). Although many eukaryotic termination factors have been identified to date, the details of the precise molecular mechanisms governing termination remain to be elucidated. To tease apart these details, we have devised an in vitro transcription system to assay for specific Pol II termination. We show for the first time that the exonucleolytic Rat1/Rai1 complex can elicit release of stalled Pol II in vitro and can do so in the absence of other factors. We also find that Rtt103, which interacts with the Pol II C-terminal domain (CTD) and with Rat1, can rescue termination activity of an exonucleolytically deficient Rat1 mutant. In light of our findings, we posit a model whereby functional nucleolytic activity is not the feature of Rat1 that ultimately promotes termination. Degradation of the nascent transcript allows Rat1 to pursue Pol II in a guided fashion and to arrive at the site of RNA exit from Pol II. Upon this arrival, however, it is perhaps the specific and direct contact between Rat1 and Pol II that transmits the signal to terminate transcription.
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dismantling promoter driven rna polymerase ii transcription complexes in vitro by the termination factor rat1
Journal of Biological Chemistry, 2013Co-Authors: Erika L Pearson, Claire MooreAbstract:Proper RNA polymerase II (Pol II) transcription termination is essential to generate stable transcripts, to Prevent Interference at downstream loci, and to recycle Pol II back to the promoter (1-3). As such, termination is an intricately controlled process that is tightly regulated by a variety of different cis- and trans-acting factors (4, 5). Although many eukaryotic termination factors have been identified to date, the details of the precise molecular mechanisms governing termination remain to be elucidated. We devised an in vitro transcription system to study specific Pol II termination. We show for the first time that the exonucleolytic Rat1·Rai1 complex can elicit the release of stalled Pol II in vitro and can do so in the absence of other factors. We also find that Rtt103, which interacts with the Pol II C-terminal domain (CTD) and with Rat1, can rescue termination activity of an exonucleolytically deficient Rat1 mutant. In light of our findings, we posit a model whereby functional nucleolytic activity is not the feature of Rat1 that ultimately promotes termination. Degradation of the nascent transcript allows Rat1 to pursue Pol II in a guided fashion and arrive at the site of RNA exit from Pol II. Upon this arrival, however, it is perhaps the specific and direct contact between Rat1 and Pol II that transmits the signal to terminate transcription.