Table of Contents
ISRN Molecular Biology
Volume 2013, Article ID 930216, 10 pages
http://dx.doi.org/10.1155/2013/930216
Research Article

Characterization of Histone H2A Derived Antimicrobial Peptides, Harriottins, from Sicklefin Chimaera Neoharriotta pinnata (Schnakenbeck, 1931) and Its Evolutionary Divergence with respect to CO1 and Histone H2A

1Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi 682016, Kerala, India
2Centre for Marine Living Resources and Ecology, Kakkanad, Kochi 682037, Kerala, India
3National Centre for Aquatic Animal Health (NCAAH), CUSAT, Fine Arts Avenue, Kochi 682016, Kerala, India

Received 18 April 2013; Accepted 8 May 2013

Academic Editors: M. Greenwood and H.-C. Lee

Copyright © 2013 Naveen Sathyan 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

Multiple alignment of amino acid sequence of histone H2A of N. pinnatta to the amino acid sequence of histone H2A previously reported from various organisms demonstrates the differences in N. pinnatta to other reported histone H2A proteins. Histone H2A of N. pinnatta is peculiar in having His at position 34 and Asp at position 42 from the N-terminus while in all other previously reported sequence of histone H2A, presence of Lys and Glu can be seen at the corresponding positions . Val at position 31 and Thr at position 60 in histone H2A of N. pinnatta. has been replaced by Val and Thr in vertebrates, whereas, histone H2A reported from invertebrates have Ile and Ala at corresponding positions. N. pinnatta has Val at position 63, a feature it has in common with invertebrates. Vertebrates have Ile at corresponding position.

  1. Supplementary Figure