Analysis of the nucleotide sequence of the form I ribulose-1,5-bisphos
phate carboxylase/oxygenase (RubisCO) genes (cbbL and cbbS) of the non
-sulfur purple bacterium Rhodobacter capsulatus indicated that the ded
uced amino acid sequence of the large subunit was not closely homologo
us to the large subunit from related organisms. Indeed, phylogenetic a
nalysis suggested that the large subunit protein (CbbL) more closely r
esembled the enzyme from alpha/beta/gamma purple bacteria and cyanobac
teria and is within a 'green-like' radiation of the RubisCO phylogenet
ic tree, well separated from CbbL of the related organism Rhodobacter
sphaeroides. A cbbQ gene was discovered downstream of cbbS in Rh. caps
ulatus, a gene arrangement which also appears to be limited to certain
organisms containing a 'green-like' RubisCO. Upstream, and divergentl
y transcribed from cbbLSQ, is a gene (cbbR(I)) that encodes a LysR-typ
e transcriptional activator. Phylogenetic analysis of the deduced amin
o acid sequence of CbbR(I) also suggests that this protein is quite di
stinct from the Rh. sphaeroides CbbR protein, and is even distinct fro
m the previously described CbbR(II) protein, the gene of which is upst
ream and divergently transcribed from the cbb(II) operon of Rh. capsul
atus. Interestingly, Rh. capsulatus CbbR(I) is more closely related to
CbbR from bacteria whose RubisCO falls within the 'green-like' radiat
ion of the CbbL tree. These studies suggest that the cbbR(I)-cbbL-cbbS
-cbbQ genes were acquired by Rh. capsulatus via horizontal gene transf
er from a bacterial species containing a 'green-like' RubisCO.