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Archaea
Volume 2012, Article ID 719092, 12 pages
http://dx.doi.org/10.1155/2012/719092
Research Article

DNA Binding in High Salt: Analysing the Salt Dependence of Replication Protein A3 from the Halophile Haloferax volcanii

Centre for Genetics and Genomics, University of Nottingham, Queen’s Medical Centre, Nottingham NG7 2UH, UK

Received 9 May 2012; Accepted 18 June 2012

Academic Editor: Yoshizumi Ishino

Copyright © 2012 Jody A. Winter 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 1: Sequence alignment of HvRPA3 with archaeal homologues using Clustal v2.0.12 on default settings and Boxshade v3.21. Brown boxes indicate the positions of the two OB-folds in MacRPA3, blue arrow the position of the HvRPA3 OB-fold. Additional labelled elements indicate the zinc ligands (red arrows) and N-terminal dimerisation domain (blue box).

Supplementary Table 2: Percentage amino acid usage over the OB-fold domains. Blue indicates residues discussed in the main text.

Supplementary Figure 3: Electrostatic surface potential of the HvRPA3 OB-fold model compared to related structures scaled at -10 kBT/e (red) to +10 kBT/e (blue). Human RPA70 shows a single OB-fold for clarity, with a 4mer stretch of oligonucleotide in stick representation in yellow. Produced using APBS and PyMol.

  1. Supplementary Materials