PMID: 12757947May 22, 2003Paper

Origin and evolution of transmembrane Chl-binding proteins: hydrophobic cluster analysis suggests a common one-helix ancestor for prokaryotic (Pcb) and eukaryotic (LHC) antenna protein superfamilies

FEMS Microbiology Letters
Laurence GarczarekFrédéric Partensky

Abstract

All chlorophyll (Chl)-binding proteins constituting the photosynthetic apparatus of both prokaryotes and eukaryotes possess hydrophobic domains, corresponding to membrane-spanning alpha-helices (MSHs). Hydrophobic cluster analysis of representative members of the different Chl protein superfamilies revealed that all Chl proteins except the five-helix reaction center II proteins and the small subunits of photosystem I possess related domains. As a major conclusion, we found that the eukaryotic antennae likely share a common precursor with the prokaryotic Chl a/b antennae from Chl-b-containing oxyphotobacteria. From these data, we propose a global scheme for the evolution of these proteins from a one-MSH ancestor.

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Citations

Jun 3, 2009·Microbiology and Molecular Biology Reviews : MMBR·D J ScanlanF Partensky
Aug 23, 2006·Proceedings of the National Academy of Sciences of the United States of America·Armen Y MulkidjanianMichael Y Galperin
Mar 29, 2011·Annual Review of Plant Biology·Martin F Hohmann-Marriott, Robert E Blankenship
Dec 5, 2014·PLoS Computational Biology·Hua ChengNick V Grishin
Sep 14, 2007·DNA Sequence : the Journal of DNA Sequencing and Mapping·Xue LiangYi Cao
Jun 25, 2005·Photosynthesis Research·Alexander N Melkozernov, Robert E Blankenship
Jun 16, 2018·Scientific Reports·Frédéric PartenskyJosé L Garrido

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