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Archaea
Volume 2013, Article ID 373275, 14 pages
http://dx.doi.org/10.1155/2013/373275
Review Article

Protein Adaptations in Archaeal Extremophiles

1Department of Chemistry, Idaho State University, Pocatello, ID 83209, USA
2Department of Biological Sciences, Idaho State University, Pocatello, ID 83209, USA

Received 24 June 2013; Revised 26 July 2013; Accepted 14 August 2013

Academic Editor: Kyung Mo Kim

Copyright © 2013 Christopher J. Reed et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary Figure: Protein sequence alignment for the archaeal cysteinyl-tRNA synthetases. The sequences represented above are: Halobacterium. salinarum (Hs), Pyrococcus furiosis (Pf), Methanlobus psychrophilus (Mp) CysRS and Escherichia coli CysRS (Ec). These sequences have been choosen to be our "model" proteins for archaeal adaptation. This alignment was constructed from a larger alignment, which used 3 examples of each protein adaptation category and was built using HMMER3 (see supplemental text) [110]. Features that are conserved in the CysRS, like the HIGH and KMSKS domain, are highlighted in green. The features that were judged to be unique to their adaptation were highlighted in the following colors: halophilic features- pink, thermophilic features- red and psychrophilic features- blue.

  1. Supplementary Figure