By Cavicchioli, Ricardo
This path-breaking publication absolutely describes the molecular mobile biology of the archaea in a single obtainable and readable quantity. With twenty-three chapters by means of the world's best specialists, this booklet emphasizes every one author's person study services, whereas additionally being a basic advisor to the newest wisdom on archaea.
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Extra resources for Archaea : molecular and cellular biology
B) Schematic model of the complex with dimensions. (C) Schematic model of the cell surface of Staphylothermus. (D) Proposed folding topology with cysteine residues and the unique proline residue separating left- and right-handed supercoils. Figure compiled and reproduced from Current Biology (259) and the Journal of Molecular Biology (302) with permission of the publishers. 24 KLETZIN Figure 6. Flagellated archaea. (A) Thermococcus celer. Reproduced from Bergey’s Manual of Systematic Bacteriology (208) with permission of the publisher.
Figure compiled and reproduced from Current Biology (259) and the Journal of Molecular Biology (302) with permission of the publishers. 24 KLETZIN Figure 6. Flagellated archaea. (A) Thermococcus celer. Reproduced from Bergey’s Manual of Systematic Bacteriology (208) with permission of the publisher. (B) Thermoplasma acidophilum. Reproduced from the Journal of Bacteriology (31) with permission of the publisher. (C) Halobacterium salinarum PHH4. Photograph courtesy of T. Hechler, Darmstadt. voltae the flagellum is composed of four proteins: FlaA, FlaB1, FlaB2, and FlaB3.
The archaeal and eucaryal EF-2s contain diphthamide, a posttranslationally modiﬁed histidine, which is the target of the toxin (Fig. 9) (175) (see Chapter 11). A short region that contains a histidine residue in EF-2 proteins is absent in the homologous EF-G protein from Bacteria, thereby rendering Bacteria resistant to the toxin (232). The in vivo role of diphthamide is not clear. Sulfolobus and yeast EF-2 overproduced in Escherichia coli contain the unmodified histidine, and these recombinant proteins had indistinguishable stability and in vitro translation activity from the diphthamide-containing native enzymes (68).