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
In: FEMS microbiology letters, Jg. 222 (2003), Heft 1, S. 59-68
Online
academicJournal
- print, 44 ref
Zugriff:
All chlorophyll (Chl)-binding proteins constituting the photosynthetic apparatus of both prokaryotes and eukaryotes possess hydrophobic domains, corresponding to membrane-spanning α-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 Ch1-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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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
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Autor/in / Beteiligte Person: | GARCZAREK, Laurence ; POUPON, Anne ; PARTENSKY, Frédéric |
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Zeitschrift: | FEMS microbiology letters, Jg. 222 (2003), Heft 1, S. 59-68 |
Veröffentlichung: | Oxford: Blackwell, 2003 |
Medientyp: | academicJournal |
Umfang: | print, 44 ref |
ISSN: | 0378-1097 (print) |
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