Bioenergetics of archaea: ATP synthesis under harsh environmental conditions.
Archaea are a heterogeneous group of microorganisms that often thrive under harsh environmental conditions such as high temperatures, extreme pHs and high salinity. As other living cells, they use chemiosmotic mechanisms along with substrate level phosphorylation to conserve energy in form of ATP. Because some archaea are rooted close to the origin in the tree of life, these unusual mechanisms are considered to have developed very early in the history of life and, therefore, may represent first energy-conserving mechanisms. A key component in cellular bioenergetics is the ATP synthase. The enzyme from archaea represents a new class of ATPases, the A1A0 ATP synthases. They are composed of two domains that function as a pair of rotary motors connected by a central and peripheral stalk(s). The structure of the chemically-driven motor (A1) was solved by small-angle X-ray scattering in solution, and the structure of the first A1A0 ATP synthases was obtained recently by single particle analyses. These studies revealed novel structural features such as a second peripheral stalk and a collar-like structure. In addition, the membrane-embedded electrically-driven motor (A0) is very different in archaea with sometimes novel, exceptional subunit composition and coupling stoichiometries that may reflect the differences in energy-conserving mechanisms as well as adaptation to temperatures at or above 100 degrees C.
Müller
V
V
Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt/Main, Campus Riedberg, Frankfurt a. Main, Germany. vmueller@em.uni-frankfurt.de
Lemker
T
T
Lingl
A
A
Weidner
C
C
Coskun
U
U
Grüber
G
G
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001105:Archaea / Q000502:physiology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D005075:Biological Evolution; D019281:Dimerization; D004734:Energy Metabolism; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
D019843:Archaeal Proteins; D021122:Protein Subunits; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases