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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / genetics*
-
Bacterial Proteins / metabolism
-
Carrier Proteins / chemistry
-
Carrier Proteins / genetics
-
Carrier Proteins / metabolism
-
Chlorophyll / metabolism*
-
Evolution, Molecular*
-
Hydrophobic and Hydrophilic Interactions
-
Light-Harvesting Protein Complexes
-
Membrane Proteins / chemistry
-
Membrane Proteins / genetics
-
Membrane Proteins / metabolism
-
Molecular Sequence Data
-
Photosynthesis / physiology
-
Photosynthetic Reaction Center Complex Proteins / chemistry
-
Photosynthetic Reaction Center Complex Proteins / genetics*
-
Photosynthetic Reaction Center Complex Proteins / metabolism
-
Photosystem I Protein Complex
-
Protein Binding / genetics
-
Protein Structure, Secondary
Substances
-
Bacterial Proteins
-
Carrier Proteins
-
Light-Harvesting Protein Complexes
-
Membrane Proteins
-
Photosynthetic Reaction Center Complex Proteins
-
Photosystem I Protein Complex
-
Chlorophyll