@article {509431,
	title = {Phylogenetic analyses of the core antenna domain: investigating the origin of photosystem I},
	journal = {J Mol Evol},
	volume = {60},
	number = {2},
	year = {2005},
	note = {<p>Mix, Lucas JHaig, DavidCavanaugh, Colleen MengResearch Support, U.S. Gov{\textquoteright}t, Non-P.H.S.2005/03/24 09:00J Mol Evol. 2005 Feb;60(2):153-63.</p>},
	month = {Feb},
	pages = {153-63},
	abstract = {<p>Phototrophy, the conversion of light to biochemical energy, occurs throughout the Bacteria and plants, however, debate continues over how different phototrophic mechanisms and the bacteria that contain them are related. There are two types of phototrophic mechanisms in the Bacteria: reaction center type 1 (RC1) has core and core antenna domains that are parts of a single polypeptide, whereas reaction center type 2 (RC2) is composed of short core proteins without antenna domains. In cyanobacteria, RC2 is associated with separate core antenna proteins that are homologous to the core antenna domains of RC1. We reconstructed evolutionary relationships among phototrophic mechanisms based on a phylogeny of core antenna domains/proteins. Core antenna domains of 46 polypeptides were aligned, including the RC1 core proteins of heliobacteria, green sulfur bacteria, and photosystem I (PSI) of cyanobacteria and plastids, plus core antenna proteins of photosystem II (PSII) from cyanobacteria and plastids. Maximum likelihood, parsimony, and neighbor joining methods all supported a single phylogeny in which PSII core antenna proteins (PsbC, PsbB) arose within the cyanobacteria from duplications of the RC1-associated core antenna domains and accessory antenna proteins (IsiA, PcbA, PcbC) arose from duplications of PsbB. The data indicate an evolutionary history of RC1 in which an initially homodimeric reaction center was vertically transmitted to green sulfur bacteria, heliobacteria, and an ancestor of cyanobacteria. A heterodimeric RC1 (=PSI) then arose within the cyanobacterial lineage. In this scenario, the current diversity of core antenna domains/proteins is explained without a need to invoke horizontal transfer.</p>},
	keywords = {Amino Acid Sequence, Bacteria/classification/*genetics/*metabolism, Evolution, Molecular, Molecular Sequence Data, Photobiology, Photosystem I Protein Complex/chemistry/*genetics/metabolism, Phylogeny, Protein Structure, Tertiary, Sequence Homology, Amino Acid},
	isbn = {0022-2844 (Print)0022-2844 (Linking)},
	author = {Mix, L. J. and Haig, D. and Cavanaugh, C. M.}
}
