title: Evidence for the presence of key chlorophyll-biosynthesis-related proteins in the genus Rubrobacter (Phylum Actinobacteria) and its implications for the evolution and origin of photosynthesis.
abstract: Homologs showing high degree of sequence similarity to the three subunits of the protochlorophyllide oxidoreductase enzyme complex (viz. BchL, BchN, and BchB), which carries out a central role in chlorophyll-bacteriochlorophyll (Bchl) biosynthesis, are uniquely found in photosynthetic organisms. The results of BLAST searches and homology modeling presented here show that proteins exhibiting a high degree of sequence and structural similarity to the BchB and BchN proteins are also present in organisms from the high G+C Gram-positive phylum of Actinobacteria, specifically in members of the genus Rubrobacter (R. x ylanophilus and R. r adiotolerans). The results presented exclude the possibility that the observed BLAST hits are for subunits of the nitrogenase complex or the chlorin reductase complex. The branching in phylogenetic trees and the sequence characteristics of the Rubrobacter BchB/BchN homologs indicate that these homologs are distinct from those found in other photosynthetic bacteria and that they may represent ancestral forms of the BchB/BchN proteins. Although a homolog showing high degree of sequence similarity to the BchL protein was not detected in Rubrobacter, another protein, belonging to the ParA/Soj/MinD family, present in these bacteria, exhibits high degree of structural similarity to the BchL. In addition to the BchB/BchN homologs, Rubrobacter species also contain homologs showing high degree of sequence similarity to different subunits of magnesium chelatase (BchD, BchH, and BchI) as well as proteins showing significant similarity to the BchP and BchG proteins. Interestingly, no homologs corresponding to the BchX, BchY, and BchZ proteins were detected in the Rubrobacter species. These results provide the first suggestive evidence that some form of photosynthesis either exists or was anciently present within the phylum Actinobacteria (high G+C Gram-positive) in members of the genus Rubrobacter. The significance of these results concerning the origin of the Bchl-based photosynthesis is also discussed.
authors.affiliation: Department of Biochemistry, McMaster University, Hamilton, ON, L8N 3Z5, Canada. gupta@mcmaster.ca.
authors.forename: Radhey S
authors.initials: RS
authors.lastname: Gupta
authors.affiliation: Department of Biochemistry, McMaster University, Hamilton, ON, L8N 3Z5, Canada.
authors.forename: Bijendra
authors.initials: B
authors.lastname: Khadka
mesh_terms: D039903:Actinobacteria / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D005075:Biological Evolution; D002734:Chlorophyll / Q000096:biosynthesis*; D018360:Crystallography, X-Ray; D016013:Likelihood Functions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000378:metabolism; D010788:Photosynthesis; D010802:Phylogeny; D021122:Protein Subunits / Q000378:metabolism; D015203:Reproducibility of Results; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D002734:Chlorophyll; D044925:Oxidoreductases Acting on CH-CH Group Donors; C023886:protochlorophyllide reductase
keywords: BchL-B-N homologs; Chlorophyll-bacteriochlorophyll (Bchl) biosynthesis; Genus Rubrobacter (phylum Actinobacteria); Origin of photosynthesis; ParA-MinD proteins; Photosynthetic phyla of bacteria