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Oxidative control of oligomeric structure formation in Vibrio cholerae cryptochrome 1 (549.2)
Author(s) -
Velez Julian,
Gindt Yvonne
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.549.2
Subject(s) - cryptochrome , vibrio cholerae , microbiology and biotechnology , chemistry , oxidative phosphorylation , biology , biochemistry , circadian clock , gene , genetics , bacteria
Cryptochrome is a member of the blue‐light photoreceptor family, and it appears to play a role in the regulation of the circadian rhythm in organisms. The oligomeric structure of the protein appears to play a key role in the signaling mechanism. Vibrio cholerae Cryptochrome 1 (VcCry1) will be used as model protein for this study; it may be involved in both DNA repair and blue‐light signaling in vivo. From our preliminary data, the oligomeric structure in VcCry1 appears to be related to the oxidation state of the active site FAD cofactor. Chemical cross linking will be used to examine the link between FAD oxidation state and oligomeric structure.