Fluorescence images of yeast cells showing mitochondria in red and two subunits of a presumed trimeric complex in green (left images: Rho5‐GFP, right images: Dck1‐GFP). Plasma membrane localization of the latter observed under standard growth conditions (upper row) is rapidly switched to mitochondria after application of oxidative stress. For details, see the article by Schmitz et al. on pp. 306–324 of this issue.

Publisher： John Wiley & Sons Inc

E-ISSN： 1365-2958|96|2|i-i

ISSN： 0950-382x

Source： MOLECULAR MICROBIOLOGY, Vol.96, Iss.2, 2015-04, pp. : i-i

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In the cyanobacterium Synechocystis sp PCC6803 the repair protease FtsH2 is located in the thylakoid membranes, but has a different distribution from the photosynthetic reaction centers suggesting the existence of dedicated repair zones. False‐color 3D surface plots from fluorescence micrographs show the distribution of fluorescence from chlorophyll (left) and GFP‐tagged FtsH2 (right) in cells grown under low light (top) or high light (bottom). For details, see the article by Sacharz et al. on pp. 448–462 of this issue.

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A montage of images through the division septum of E. coli cells. The images were captured by dual‐color time‐gated Stimulated Emission Depletion (STED) nanoscopy, on cells simultaneously expressing FtsZ‐mNeonGreen (green) and mStrawberry‐FtsN (red). The images show that FtsZ and FtsN are spatially separated. For details, see the article by Söderström et al. on pp. 387‐401 of this issue.

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DdrO regulates the radiation desiccation response and apoptotic‐like cell death in the Deinococcus radiodurans. Light microscopy was used to visualize the effects of depleting the DdrO repressor on D. radiodurans morphology (left to right): Nomarski interference contrast (DIC), membrane staining (FM4‐64), DNA staining (DAPI), and merged images. The cells were depleted of DrdO from 8h (top), 16 h (middle), or 24 h (bottom). DdrO‐depleted cells display morphological changes evocative of an apoptotic‐like response including DNA condensation and vesicle formation. For details, see the article by Devigne et al. on pp. 1069–1084 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 96, Iss. 5, 2015-06 ,pp. : i-i

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Structure of Bacillus anthracis AtxA, a dimeric virulence regulator, with one subunit color‐coded and one in gray. AtxA contains two phosphoenolpyruvate:carbohydrate phosphotransferase system‐related domains (PRD1 and PRD2; blue and green) and two helix‐turn‐helix (HTH) containing DNA‐binding domains (red and purple). Two histidines that are phosphorylated are highlighted in one of the subunits of the dimer. For details, see the article by Hammerstrom et al. on pp. 426–441 of this issue

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Molecular modeling of the Trypanosoma brucei aminopurine transporter P2/TbAT1, implicated in resistance to both diamidine and melaminophenyl arsenical classes of drugs, predicts that residues F19 (left), D140 (top) and F316 (right) interact with substrates. The binding site of adenosine (green carbon atoms) and diminazene (yellow carbon atoms) is shown with hydrogen bonds between Asp140 and bound adenosine in dashed blue lines. For details, see the article by Munday et al. on pp. 887–900 of this issue.

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