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Characterization of a family of proteins for bilin addition activity and interaction with the beta subunit of phycocyanin from synechococcus sp. PCC 7002

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Contact Information	Please send any questions regarding this item to libref@uno.edu
Title	Characterization of a family of proteins for bilin addition activity and interaction with the beta subunit of phycocyanin from synechococcus sp. PCC 7002
Author	Gallo, Eduardo, F.
Keywords	University of New Orleans. Honors thesis. 2004.; University of New Orleans. Dept. of Biological Sciences.
Abstract/Introduction	The light-harvesting phycobiliprotein C-phycocyanin from Synechococcus sp. PCC 7002 is composed of a and b subunits which bear bilins at specific cysteine residues. There is strong evidence showing that attachment of phycocyanobilin (PCB) to the a-subunit of apo-phycocyanin (apo-CpcA) is catalyzed by the heterodimeric lyase, CpcEF. However, little is known about bilin attachment to the b-subunit (CpcB). Recent studies suggest that the cpcXl, cpcX3, and cpc Y genes from this species encode proteins that are likely involved in phycobiliprotein biosynthesis and might act as a heterodimeric PCB-b-phycocyanin lyase, similar to CpcEF. In order to characterize these proteins, the cpcE gene was cloned in Escherichia coli and overexpressed as a 6x Histidine-tagged fusion protein (HT-CpcB). Purified HT-CpcB was used in a "pull-down" assay to determine whether there is protein-protein interaction between HT-CpcB and CpcX 1, CpcX3, and CpcY. PCB addition assays were also performed to determine if the presence of these proteins results in correct PCB addition to apo-CpcB. Some interaction was observed between HT-CpcB and CpcXl and between HT-CpcB and CpcX3. Bilin addition in the presence of the putative lyases was diminished when compared to a control lacking the lyases. This suggests that these proteins are limiting access of PCB to apo-CpcB for spontaneous addition. It is possible that other subunits are required to achieve the appropriate conformation for correct bilin addition. Therefore, additional experiments are necessary to more rigorously characterize these proteins. Nonetheless, this study describes the first attempts to characterize the biochemical interactions among these putative lyases and a phycobiliprotein, while suggesting new methods to examine whether these proteins are involved in correct bilin addition to apo-CpcB.
Access	PDF access restricted to UNO campus only
Degree	B.S.
Degree Program	Biological Sciences
Department	Department of Biological Sciences
Thesis Advisor	Schluchter, Wendy
Advisory Committee	Clancy, Mary; Blanton, Linda Lonon
Date Degree Awarded	2004; *
Rights	The University of New Orleans and its agents retain the non-exclusive license to archive and make accessible this 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.
Notes	v, 35 leaves : ill. ; 29 cm.; typescript; "An honors thesis... in partial fulfillment of the requirements for the degree of Bachelor of Arts, with University Honors and Honors in Biological Sciences"; Vita; Thesis (B.S.)--University of New Orleans, 2004; Includes bibliographical references (leaves 34-35); May 2004; approved May 12, 2004.
Object File Name	st000149
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Characterization of a family of proteins for bilin addition activity and interaction with the beta subunit of phycocyanin from synechococcus sp. PCC 7002

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