Premium
Hypothetical Protein Synw_0921 and Copper Response in Synechococcus sp. WH8102
Author(s) -
Gnann Andrew,
George Thompson Alayna,
McEvoy Megan
Publication year - 2015
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.29.1_supplement.884.67
Subject(s) - cyanobacteria , synechococcus , copper , sulfur , cysteine , chemistry , biochemistry , biophysics , biology , bacteria , genetics , enzyme , organic chemistry
Marine cyanobacteria account for more than 20% of global carbon fixation. Human activities significantly alter free copper concentrations in coastal waters, adversely affecting cyanobacterial populations.The protein Synw_0921 from the marine cyanobacterium Synechococcus sp. WH8102 is upregulated during growth at high copper concentrations, suggesting that Synw_0921 is involved in copper homeostasis. Homologs of Synw_0921 are found only within marine cyanobacteria. Bioinformatic analysis indicates that Synw_0921 and its homologs contain four conserved cysteine residues with no conserved protein domains. Previous work demonstrates that Synw_0921 binds an iron‐sulfur cluster, not the copper ions that we predicted. Current work seeks to characterize how the cysteine residues individually contribute to iron‐sulfur cluster binding in Synw_0921 and to determine if iron‐sulfur clusters affect copper binding. Currently, UV‐visible spectroscopy is employed to monitor characteristic iron‐sulfur absorbance around 418 nm in wild type and double cysteine mutants. Atomic absorbance spectroscopy will be used to quantify metal concentrations in protein samples, indicating differences in metal binding between wild type and double mutant forms. Additionally, crystal screens have returned a successful growth condition, and larger‐scale crystallization efforts are underway.