Evolutionary divergence of chloroplast FAD synthetase proteins.
BACKGROUND
Flavin adenine dinucleotide synthetases (FADSs) - a group of bifunctional enzymes that carry out the dual functions of riboflavin phosphorylation to produce flavin mononucleotide (FMN) and its subsequent adenylation to generate FAD in most prokaryotes - were studied in plants in terms of sequence, structure and evolutionary history.


RESULTS
Using a variety of bioinformatics methods we have found that FADS enzymes localized to the chloroplasts, which we term as plant-like FADS proteins, are distributed across a variety of green plant lineages and constitute a divergent protein family clearly of cyanobacterial origin. The C-terminal module of these enzymes does not contain the typical riboflavin kinase active site sequence, while the N-terminal module is broadly conserved. These results agree with a previous work reported by Sandoval et al. in 2008. Furthermore, our observations and preliminary experimental results indicate that the C-terminus of plant-like FADS proteins may contain a catalytic activity, but different to that of their prokaryotic counterparts. In fact, homology models predict that plant-specific conserved residues constitute a distinct active site in the C-terminus.


CONCLUSIONS
A structure-based sequence alignment and an in-depth evolutionary survey of FADS proteins, thought to be crucial in plant metabolism, are reported, which will be essential for the correct annotation of plant genomes and further structural and functional studies. This work is a contribution to our understanding of the evolutionary history of plant-like FADS enzymes, which constitute a new family of FADS proteins whose C-terminal module might be involved in a distinct catalytic activity.
Estación Experimental de Aula Dei, Consejo Superior de Investigaciones Científicas (CSIC), Avda. Montañana, Zaragoza, Spain. yruela@eead.csic.es
Inmaculada
I
Yruela
Sonia
S
Arilla-Luna
Milagros
M
Medina
Bruno
B
Contreras-Moreira
D000595:Amino Acid Sequence; D019295:Computational Biology; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry / Q000235:genetics*; D009713:Nucleotidyltransferases / Q000737:chemistry / Q000235:genetics*; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics*; D010944:Plants / Q000145:classification* / Q000201:enzymology* / Q000235:genetics; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D009097:Multienzyme Complexes; D010940:Plant Proteins; C023114:FAD synthetase complex; D009713:Nucleotidyltransferases