Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 389, Issue 4, Pages 602-606Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.09.030
Keywords
Bilin lyase; Complementary chromatic adaptation; Morphology; Photosensing; Phycobiliprotein
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Funding
- National Science Foundation [MCB-0643516]
- U.S. Department of Energy [DE-FG02-91ER20021]
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Cyanobacteria harvest light for photosynthesis using photosynthetic light-harvesting complexes called phycobilisomes (PBSs). Lyases are enzymes responsible for covalent attachment of light-absorbing chromophores to the phycobiliproteins (PBPs) contained in PBSs. We isolated a pigmentation mutant in the filamentous cyanobacterium Fremyella diplosiphon and determined that it possesses an insertional mutation in cpcF, which encodes one component of a heterodimeric phycocyanin lyase. Here, we discuss the implications of the mutation in cpcF on light-dependent pigmentation and Morphology responses characteristic of complementary chromatic adaptation in F diplosiphon. Although cpcF encodes a phycocyanin lyase, significant decreases in the levels of all classes of PBPs are associated with CpcF deficiency in F. diplosiphon. Notably, CpcF deficiency has a limited effect on the shape of F diplosiphon cells, but significantly impacts filament length. Possible mechanisms for the broad impact of CpcF deficiency on pigmentation and filament morphology are discussed. (C) 2009 Elsevier Inc. All rights reserved.
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