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Transcript
Supplementary Figure 1 Domain structure of the MamJ protein
The 426 aa protein with a calculated mass of 44.3 kDa and isoelectric point of 3.9
contains several domains with highly biased amino acid composition. The central
acidic domain contains two identical Glu-rich stretches (81-168 and 169-256) that are
arranged as tandem repeats (acidic aa, red; basic aa, yellow; hydrophobic aa, black;
hydrophilic aa except Glu and Asp, purple). Within the acidic domain, Glu and Asp
residues are predominantly located between position 224 and 294, accounting for
32.4% of all amino acid residues within that region.
Supplementary Figure 2 Molecular organization of the mamAB cluster in the
wild type and ΔmamJ
The mamJ gene (red) is located within the mamAB cluster encompassing 17 ORFs (a).
An unmarked in frame deletion mutant ΔmamJ strain was generated by homologous
recombination between the chromosome and the suicide vector pAS2 harbouring
flanking sequence regions of mamJ (upstream fragment ASmamJu_f/ASmamJs_r;
downstream fragment ASmamJe_f/ASmamJd_r). By double crossover mamJ is
deleted from the mamAB cluster in the mutant (b). Recombining sequences on pAS2
were designed to preserve mamJ start and stop codon.
Supplementary Figure 3 Cryo-ET of a wild type cell showing a chain of mature
magnetosome crystals located adjacent to the cytoplasmic membrane
Three-dimensional reconstruction of a vitrified magnetic wild type cell showing the
location of a magnetosome chain within the cell. In x-y slices magnetosomes form a
chain located at midcell with small crystals at the chain ends (I). While in x-y the
chain follows the concave cell boundary, the magnetosomes are located adjacent to
membrane in x-z view (II) at the position indicated by the arrow in (I). Chain of
magnetosomes is slightly curved as illustrated in y-z view (III). Surface-rendered
representation of the cell showing the magnetite crystals (auburn) forming a curved
chain adjacent to the membrane (blue). Mesh depicts the modeled outline of the
complete membrane (IV).