PMID- 9873077
OWN - NLM
STAT- MEDLINE
DCOM- 19990527
LR  - 20190905
IS  - 0022-2844 (Print)
IS  - 0022-2844 (Linking)
VI  - 48
IP  - 1
DP  - 1999 Jan
TI  - A phylogenetic assessment of the eukaryotic light-harvesting antenna proteins, 
      with implications for plastid evolution.
PG  - 59-68
AB  - The light-harvesting complexes (LHCs) are a superfamily of chlorophyll-binding 
      proteins present in all photosynthetic eukaryotes. The Lhc genes are 
      nuclear-encoded, yet the pigment-protein complexes are localized to the thylakoid 
      membrane and provide a marker to follow the evolutionary paths of plastids with 
      different pigmentation. The LHCs are divided into the chlorophyll a/b-binding 
      proteins of the green algae, euglenoids, and higher plants and the chlorophyll 
      a/c-binding proteins of various algal taxa. This work examines the phylogenetic 
      position of the LHCs from three additional taxa: the rhodophytes, the 
      cryptophytes, and the chlorarachniophytes. Phylogenetic analysis of the LHC 
      sequences provides strong statistical support for the clustering of the 
      rhodophyte and cryptomonad LHC sequences within the chlorophyll a/c-binding 
      protein lineage, which includes the fucoxanthin-chlorophyll proteins (FCP) of the 
      heterokonts and the intrinsic peridinin-chlorophyll proteins (iPCP) of the 
      dinoflagellates. These associations suggest that plastids from the heterokonts, 
      haptophytes, cryptomonads, and the dinoflagellate, Amphidinium, evolved from a 
      red algal-like ancestor. The Chlorarachnion LHC is part of the chlorophyll 
      a/b-binding protein assemblage, consistent with pigmentation, providing further 
      evidence that its plastid evolved from a green algal secondary endosymbiosis. The 
      Chlorarachnion LHC sequences cluster with the green algal LHCs that are 
      predominantly associated with photosystem II (LHCII). This suggests that the 
      green algal endosymbiont that evolved into the Chlorarachnion plastid was 
      acquired following the emergence of distinct LHCI and LHCII complexes.
FAU - Durnford, D G
AU  - Durnford DG
AD  - Department of Biology, University of New Brunswick, Mail Service #45111, 
      Fredericton, New Brunswick E3B 6E1, Canada. durnford@unb.ca
FAU - Deane, J A
AU  - Deane JA
FAU - Tan, S
AU  - Tan S
FAU - McFadden, G I
AU  - McFadden GI
FAU - Gantt, E
AU  - Gantt E
FAU - Green, B R
AU  - Green BR
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - J Mol Evol
JT  - Journal of molecular evolution
JID - 0360051
RN  - 0 (Carrier Proteins)
RN  - 0 (Light-Harvesting Protein Complexes)
RN  - 0 (Photosynthetic Reaction Center Complex Proteins)
RN  - 0 (Photosystem II Protein Complex)
RN  - 0 (fucoxanthin-, chlorophyll a-c-containing protein)
SB  - IM
MH  - Amino Acid Sequence
MH  - Carrier Proteins/chemistry/*genetics
MH  - Chloroplasts/*genetics
MH  - *Evolution, Molecular
MH  - *Light-Harvesting Protein Complexes
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Photosynthetic Reaction Center Complex Proteins/*genetics
MH  - Photosystem II Protein Complex
MH  - *Phylogeny
MH  - Plants/classification/*genetics
MH  - Sequence Homology, Amino Acid
EDAT- 1999/01/05 00:00
MHDA- 1999/01/05 00:01
CRDT- 1999/01/05 00:00
PHST- 1999/01/05 00:00 [pubmed]
PHST- 1999/01/05 00:01 [medline]
PHST- 1999/01/05 00:00 [entrez]
AID - 10.1007/pl00006445 [doi]
PST - ppublish
SO  - J Mol Evol. 1999 Jan;48(1):59-68. doi: 10.1007/pl00006445.