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Mitochondrial membrane fusion research progress

Posted by star on 2018-08-22 01:49:18
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Recently, the study has found that the mitochondrial fusion protein MFN1 is a self-mediating fusion protein and revealing MFN1 targeted to the mitochondrial outer membrane of the important elements, as well as MFN1 protein C-terminal amphipathic helix on its fusion function plays an important role for Homologous membrane fusion mechanism.

Mitochondria are organelles surrounded by bilayer membranes and present dispersed network structures in mammalian cells, providing an important place for the life activities of cells. Mitochondrial morphology and function are closely related and require continued integration and division to maintain its shape and function. The proteins that mediate mitochondrial fusion and cleavage are mainly derived from the dynamin family and possess GTPase activity. The protein that mediates mitochondrial outer membrane fusion in mammalian cells is Mitofusin (MFN), also MFN1 and MFN2 have been identified. Mitochondria are fragmented by the separate deletion of these two genes in the cell and knocking out MFN1 or MFN2 in mice results in lethality of the embryo. Mutations in MFN2 lead to a neurodegenerative disease, Charcot-Marie Tooth Syndrome (CMT2A). However, the mechanisms which they mediate homologous membrane fusion remain unclear due to the difficulty of purification and recombination of full-length MFN proteins.

It has been found that MFN1 and Atlastin (ATL), which mediate the fusion of endoplasmic reticulum, have a very similar structural membrane sequence with a N-terminal GTPase domain located in the cytoplasmic domain, a helical bundle domain, a transmembrane domain and a C- Cytoplasmic tail. Since the mechanism of ATL1-mediated membrane fusion has been well studied, the team constructed a series of chimeric proteins of MFN1 and ATL1 to study the function of MFNs. Though the transmembrane exchange is between the two, MFN can be localized to the endoplasmic reticulum and mediate endoplasmic reticulum membrane fusion. ......

Simple exercise can reduce the risk of heart disease

Posted by star on 2018-08-22 01:41:29
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There is plenty of evidence that regular exercise reduces the risk of heart disease and stroke, but how long does it take to show up? Maybe a few weeks, maybe months, until we lose weight and cholesterol levels drop. However, a recent article provides evidence that a single workout can have a protective effect on the heart.

Usually we think that exercise can reduce weight, reduce cholesterol, insulin levels, and fat content have the effect of prevention of cardiovascular disease, but it often take weeks or even months, and the effects are not significant. However, this article summarizes previous research and finds that a single type of exercise can protect the heart.

In many studies, scientists have suggested that rats and mice are induced to develop heart disease, and the effects of exercise on reducing the risk of heart attack have been examined, which is the proportion of tissue necrosis. Using animal experiments, the researchers found that a single workout can have a heart-healthy effect, and it can last a few days.

Exercise is thought to promote the release of bone marrow related factors, reducing the risk of heart attack. In one study, the authors extracted blood samples from people before and after exercise and imported them into the rabbit's heart. After that, the author thought that the rabbit was induced to produce the symptoms of a heart attack. The results showed that the blood in the body was more likely to reduce the risk of heart attack than before exercise.

Surprisingly, these effects were not associated with common cardiovascular risk factors, such as blood pressure, cholesterol, weight, etc, or adaptation of the body reaction, such as cardiac function enhancement. But these effects can persist for more than a few days.



E. coli chromosomal replication begins at oriC

Posted by star on 2018-08-22 01:20:53
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    When temperature-sensitive dnaA mutants are switched from nonpermissive to permissive temperatures, DNA synthesis begins at oriC. Subsequent bidirectional replication produces a gene dosage effect in which genes closest to oriC are present in twice the abundance of those further away. The OriC region of the E. coli chromosome shows oric and some of the genes that surround it at minute 84 of the E. coli genetic map.

    The E. coli chromosome's large size and fragility precludes studying oriC structure and function in the intact chromosome in vitro. Fortunately, the desired goals can be achieved by constructing a minichromosome that depends on oriC for its replication. A restriction endonuclease cuts the bacterial chromosome into fragments and the plasmid DNA into a fragment containing a drug-resistance gene (ampicillin in this example) but lacking the plasmid origin of replication. After mixing, the bacterial and plasmid DNA fragments are joined by DNA ligase and the resulting recombinant plasmid DNA is used to transform bacteria. The cells are then spread onto growth medium that contains ampicillin. Only cells bearing recombinant plasmid DNA with a drug-resistance gene and oriC will form colonies under these growth conditions. Intracellular nucleases eventually destroy DNA molecules that cannot replicate autonomously.

    The minimal sequence needed for oriC function, which was determined by trimming the ends of the cloned site, is 245 bp long. This sequence contains several elements that are essential for normal function. Five elements within the minimal sequence contain a 9 bp common sequence 5'_TTATNCACA (where N is any nucleotide). These 9-mers are called DnaA boxes because DnaA · ATp andDnaA · ADP complexes bind tightly to them. The individual DnaA boxes are designated R1-R5. DnaA also binds to three additional elements in oriC called I boxes, which also contain 9 bp. However, Dn......

The E coli initiator protein—DnaA, has four functional domains

Posted by star on 2018-08-20 23:24:03
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    A great deal is known about the E. coli initiator protein, DnaA, even though its high resolution structure has not yet been determined. Considerable structure-function information has been obtained from biochemical studies and sequence comparisons with other proteins. Based on this information, the DnaA protein can be divided into four functional domains, which are numbered I to IV starting at the amino terminus.

    Each domain plays a critical role in the initiation of DNA synthesis. Domain I participates in DnaA oligomerization and also helps to recruit the DnaB protein, a helicase containing six identical subunits that is required to unwind the double helix so that DNA synthesis can be initiated. Domain ∏binds the Dna8 helicase transiently. Domain Ⅲ binds ATP or ADP and has an ATPase activity. The DnaA · ATP complex is essential for replication initiation. Domain IV binds to the replicator and helps to unwind the double helix so that the DnaB can be loaded onto the single strands that are generated. It also contains a membrane binding site that interacts with anionic glycerophospholipids in the cell membrane. This interaction facilitates the conversion of the DnaA · ADP complex to the DnaA · ATP complex, an essential step that must take place before a new round of replication can begin.



DNA replicator

Posted by star on 2018-08-20 01:37:04
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    The replicon model proposes that a site-specific DNA-binding protein binds to a DNA sequence called a replicator.

    Although genes replicate as part of larger chromosomes, most cannot replicate as independent units. An independently replicating DNA molecule such as a viral, bacterial or eukaryotic chromosome or a plasmid that can maintain a stable presence in a cell is called a replicon.

    In the early 1960s Francois Jacob and Sydney Brenner proposed the replicon model to explain how DNA molecules replicate autonomously. The replicon model requires two specific components, an initiator protein and a replicator. The initiator protein binds to the replicator, a specific set of sequences within the DNA molecule that is to be replicated. Because the replicator must be part of the DNA that is to be replicated, it is said to be cis-acting. Once bound to the replicator the initiator helps to unwind the DNA and recruit components of the replication machinery. The specific site within the replicator at which replication initiated is called the origin of replication. Bacterial cells usually require just one origin of replication, which in E. coli is called oriC. Because a bacterial replicator is usually quite short (200 to 300 bp), the terms replicator and origin of replication tend to be used interchangeably even though technically the origin of replication is just a part of the replicator. Eukaryotes, which have much longer chromosomes than bacteria, require many origins of replication.



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