CpcF-dependent regulation of pigmentation and development in Fremyella diplosiphon.
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.
Whitaker
Melissa J
MJ
Department of Energy-Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.
Bordowitz
Juliana R
JR
Montgomery
Beronda L
BL
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D000458:Cyanobacteria / Q000166:cytology / Q000235:genetics / Q000254:growth & development*; D008969:Molecular Sequence Data; D010858:Pigmentation / Q000235:genetics / Q000502:physiology*
D001426:Bacterial Proteins