Blog
About

  • Record: found
  • Abstract: not found
  • Article: not found

MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria

Read this article at

ScienceOpenPublisher
Bookmark
      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

      Related collections

      Most cited references 51

      • Record: found
      • Abstract: not found
      • Article: not found

      ggplot2

        Bookmark
        • Record: found
        • Abstract: found
        • Article: not found

        Automated electron microscope tomography using robust prediction of specimen movements.

         D Mastronarde (2005)
        A new method was developed to acquire images automatically at a series of specimen tilts, as required for tomographic reconstruction. The method uses changes in specimen position at previous tilt angles to predict the position at the current tilt angle. Actual measurement of the position or focus is skipped if the statistical error of the prediction is low enough. This method allows a tilt series to be acquired rapidly when conditions are good but falls back toward the traditional approach of taking focusing and tracking images when necessary. The method has been implemented in a program, SerialEM, that provides an efficient environment for data acquisition. This program includes control of an energy filter as well as a low-dose imaging mode, in which tracking and focusing occur away from the area of interest. The program can automatically acquire a montage of overlapping frames, allowing tomography of areas larger than the field of the CCD camera. It also includes tools for navigating between specimen positions and finding regions of interest.
          Bookmark
          • Record: found
          • Abstract: found
          • Article: not found

          A bacterial two-hybrid system based on a reconstituted signal transduction pathway.

          We describe a bacterial two-hybrid system that allows an easy in vivo screening and selection of functional interactions between two proteins. This genetic test is based on the reconstitution, in an Escherichia coli cya strain, of a signal transduction pathway that takes advantage of the positive control exerted by cAMP. Two putative interacting proteins are genetically fused to two complementary fragments, T25 and T18, that constitute the catalytic domain of Bordetella pertussis adenylate cyclase. Association of the two-hybrid proteins results in functional complementation between T25 and T18 fragments and leads to cAMP synthesis. Cyclic AMP then triggers transcriptional activation of catabolic operons, such as lactose or maltose, that yield a characteristic phenotype. In this genetic test, the involvement of a signaling cascade offers the unique property that association between the hybrid proteins can be spatially separated from the transcriptional activation readout. This permits a versatile design of screening procedures either for ligands that bind to a given "bait," as in the classical yeast two-hybrid system, or for molecules or mutations that block a given interaction between two proteins of interest.
            Bookmark

            Author and article information

            Journal
            Nature Microbiology
            Nat Microbiol
            Springer Science and Business Media LLC
            2058-5276
            July 29 2019
            10.1038/s41564-019-0512-8
            © 2019

            http://www.springer.com/tdm

            Comments

            Comment on this article