Date of Award
Spring 5-2013
Degree Type
Thesis
Degree Name
M.S.
Degree Program
Biological Sciences
Department
Biological Sciences
Major Professor
Schluchter, Wendy
Second Advisor
Liu, Zhengchang
Third Advisor
Clancy, Mary
Abstract
Phycoerythrin (PE) present on the outer phycobilisome (PBS) rods in Fremyella diplosiphon contains covalently attached phycoerythrobilin (PEB) chromophores for efficient photosynthetic light capture. Chromophore ligation on phycobiliprotein subunits occurs through bilin lyase catalyzed reactions. The cpeY and cpeZ genes in F. diplosiphon were shown to attach PEB on alph-82 of PE. To better understand the individual functions of cpeY and cpeZ in native cyanobacteria, we characterized PBS and PE purified from cpeY and cpeZ deletion mutants and compared them with wild type (WT). Both cpeY and cpeZ mutants generated much less PE than WT as well as assembling much less PE into the PBS. PE purified from cpeY mutant had phycocyanobilin on alpha-PE in place of PEB. The mutation of cpeZ affected the biosynthesis and accumulation of beta-PE with a red-shifted absorbance compared to WT PE. CpeY was shown to function as a bilin lyase, and CpeZ possibly functions as a chaperone.
Recommended Citation
Kronfel, Christina M., "Characterization of cpeY and cpeZ mutants in Fremyella diplosiphon strain UTEX 481" (2013). University of New Orleans Theses and Dissertations. 1642.
https://scholarworks.uno.edu/td/1642
Rights
The University of New Orleans and its agents retain the non-exclusive license to archive and make accessible this dissertation or thesis in whole or in part in all forms of media, now or hereafter known. The author retains all other ownership rights to the copyright of the thesis or dissertation.