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- Aquaporins (AQPs) are membrane channel proteins found in a wide range of organisms, from archaea and bacteria to plants and animals. AQPs facilitate the rapid transport of water across cellular membranes and are of fundamental importance to the control of cell volume and transcellular water traffic.
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Home > CUNY Graduate Center > Publications and Research > 362
It takes FASTA DNA sequence as input, and write GFF3 as output. It uses the new NHMMER tool that comes with HMMER 3.1 for HMM searching in RNA:DNA style. NHMMER binaries for 64-bit Linux and Mac OS X are included and will be auto-detected. Multithreading is supported and one can expect roughly linear speed-ups with more CPUs. Bryan spears net worth.
Publications and Research
Title
Authors
Document Type
Article
Publication Date
9-29-2010
Abstract
Background: The GXGD-type diaspartyl intramembrane protease, presenilin, constitutes the catalytic core of the c-secretase multi-protein complex responsible for activating critical signaling cascades during development and for the production of b-amyloid peptides (Ab) implicated in Alzheimer’s disease. The only other known GXGD-type diaspartyl intramembrane proteases are the eukaryotic signal peptide peptidases (SPPs). The presence of presenilin-like enzymes outside eukaryots has not been demonstrated. Here we report the existence of presenilin-like GXGD-type diaspartyl intramembrane proteases in archaea.
Methodology and Principal Findings: We have employed in vitro activity assays to show that MCMJR1, a polytopic membrane protein from the archaeon Methanoculleus marisnigri JR1, is an intramembrane protease bearing the signature YD and GXGD catalytic motifs of presenilin-like enzymes. Mass spectrometry analysis showed MCMJR1 could cleave model intramembrane protease substrates at several sites within their transmembrane region. Remarkably, MCMJR1 could also cleave substrates derived from the b-amyloid precursor protein (APP) without the need of protein co-factors, as required by presenilin. Two distinct cleavage sites within the transmembrane domain of APP could be identified, one of which coincided with Ab40, the predominant site processed by c-secretase. Finally, an established presenilin and SPP transition-state analog inhibitor could inhibit MCMJR1.
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Conclusions and Significance: Our findings suggest that a primitive GXGD-type diaspartyl intramembrane protease from archaea can recapitulate key biochemical properties of eukaryotic presenilins and SPPs. MCMJR1 promises to be a more tractable, simpler system for in depth structural and mechanistic studies of GXGD-type diaspartyl intramembrane proteases.
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Biochemical and Biomolecular Engineering Commons, Biology Commons, Cell Biology Commons
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Biology Posters
Title
Authors
Document Type
Poster
Publication Date
2016
Abstract
Natural gas (methane) is emerging as a viable power source for many industrial, commercial, and domestic applications. Bio-methane provides a promising replacement for mined natural gas. https://hererfile804.weebly.com/blog/download-gsnap-autotune-vst-plugin. Methanogenic bacteria produce this bio-methane. These anaerobic bacteria pertain to the Domain Archaea, and are found in extreme environments where few other bacteria survive. They are employed by Up-Flow Anaerobic Sludge Blanket (UASB) reactors in the digestion of wastes to a marketable product (methane). The genome of methanogenic bacteria can be amplified using polymerase chain reaction (PCR), a synthetic DNA replication system. This system employs specific sequences of DNA called primers. The primers employed in this study focused on 16S rRNA amplification providing a fingerprint of the organism’s identity. Previous design of these primers was unsuccessful and resulted in non-specific binding.
Recommended Citation
Walters, Andrew; Doloman, Anna; and Miller, Charles, 'Development of Archaeal and Algalytic Bacteria Detection Systems' (2016). Latest casino bonuses free games. Biology Posters. Paper 27.
https://digitalcommons.usu.edu/biology_posters/27
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