Magnetochrome: a c-type cytochrome domain specific to magnetotatic bacteria

Biochem Soc Trans. 2012 Dec 1;40(6):1319-23. doi: 10.1042/BST20120104.

Abstract

Magnetotactic bacteria consist of a group of taxonomically, physiologically and morphologically diverse prokaryotes, with the singular ability to align with geomagnetic field lines, a phenomenon referred to as magnetotaxis. This magnetotactic property is due to the presence of iron-rich crystals embedded in lipidic vesicles forming an organelle called the magnetosome. Magnetosomes are composed of single-magnetic-domain nanocrystals of magnetite (Fe(3)O(4)) or greigite (Fe(3)S(4)) embedded in biological membranes, thereby forming a prokaryotic organelle. Four specific steps are described in this organelle formation: (i) membrane specialization, (ii) iron acquisition, (iii) magnetite (or greigite) biocrystallization, and (iv) magnetosome alignment. The formation of these magnetic crystals is a genetically controlled process, which is governed by enzyme-catalysed processes. On the basis of protein sequence analysis of genes known to be involved in magnetosome formation in Magnetospirillum magneticum AMB-1, we have identified a subset of three membrane-associated or periplasmic proteins containing a double cytochrome c signature motif CXXCH: MamE, MamP and MamT. The presence of these proteins suggests the existence of an electron-transport chain inside the magnetosome, contributing to the process of biocrystallization. We have performed heterologous expression in E. coli of the cytochrome c motif-containing domains of MamE, MamP and MamT. Initial biophysical characterization has confirmed that MamE, MamP and MamT are indeed c-type cytochromes. Furthermore, determination of redox potentials for this new family of c-type cytochromes reveals midpoint potentials of -76 and -32 mV for MamP and MamE respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Crystallization
  • Cytochrome c Group / chemistry
  • Cytochrome c Group / genetics
  • Cytochrome c Group / metabolism
  • Electron Transport
  • Magnetosomes / genetics
  • Magnetosomes / metabolism*
  • Magnetosomes / physiology
  • Magnetospirillum / genetics*
  • Magnetospirillum / metabolism
  • Magnetospirillum / physiology
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Protein Structure, Tertiary

Substances

  • Bacterial Proteins
  • Cytochrome c Group