PMID- 9037167 OWN - NLM STAT- MEDLINE DCOM- 19970324 LR - 20190822 IS - 0167-4412 (Print) IS - 0167-4412 (Linking) VI - 33 IP - 1 DP - 1997 Jan TI - LhcaR1 of the red alga Porphyridium cruentum encodes a polypeptide of the LHCI complex with seven potential chlorophyll a-binding residues that are conserved in most LHCs. PG - 157-67 AB - The accessory light-harvesting polypeptides associated with photosystem I (LHCI) in Porphyridium cruentum bind chlorophyll a, zeaxanthin and beta-carotene. A cDNA library of P. cruentum was screened with an antiserum specific to the LHCI polypeptides, and an 0.9 kb fragment was identified as coding for an LHCI polypeptide. This cDNA, which we named LhcaR1, has an open reading frame encoding 222 amino acid residues including a putative transit peptide of 28 amino acids. Hydropathy analysis suggests that there are three transmembrane helices in the mature polypeptide. Each of the amino acid residues that bind chlorophyll (six residues) and serve in stabilizing the helices in higher-plant LHCs are conserved in helices 1 and 3 of P. cruentum LhcaR1. The N-terminal flanking regions of these two helices also show high sequence conservation with other LHCs. Helix 2 contains a seventh putative chlorophyll-binding site, but resembles helix 2 of higher-plant LHCs to a lesser degree. A sequence motif of 11 residues found near the N-terminus and in each of the three helices suggests the possibility that the red algal LhcaR1 derives from a gene duplication. Polypeptides of the expected molecular weight in six other red algae (Achrochaetium, Bangia, Callithamnion, Cyanidium, Polysiphonia, Spermothamnion) were recognized by the antiserum to P. cruentum LHCI, indicating a wide distribution of LHCI in rhodophytes. FAU - Tan, S AU - Tan S AD - Department of Plant Biology, University of Maryland, College Park 20742, USA. FAU - Cunningham, F X Jr AU - Cunningham FX Jr FAU - Gantt, E AU - Gantt E LA - eng SI - GENBANK/U58679 PT - Comparative Study PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - Netherlands TA - Plant Mol Biol JT - Plant molecular biology JID - 9106343 RN - 0 (Algal Proteins) RN - 0 (Chlorophyll Binding Proteins) RN - 0 (DNA, Complementary) RN - 0 (Light-Harvesting Protein Complexes) RN - 0 (Photosynthetic Reaction Center Complex Proteins) RN - 0 (Photosystem I Protein Complex) RN - 0 (Recombinant Proteins) RN - 1406-65-1 (Chlorophyll) RN - YF5Q9EJC8Y (Chlorophyll A) SB - IM MH - *Algal Proteins MH - Amino Acid Sequence MH - Base Sequence MH - Binding Sites MH - Chlorophyll/*metabolism MH - Chlorophyll A MH - Chlorophyll Binding Proteins MH - Cloning, Molecular MH - DNA, Complementary MH - *Genes, Plant MH - *Light-Harvesting Protein Complexes MH - Molecular Sequence Data MH - Molecular Weight MH - Open Reading Frames MH - Photosynthetic Reaction Center Complex Proteins/*biosynthesis/chemistry/genetics MH - *Photosystem I Protein Complex MH - Protein Structure, Secondary MH - Recombinant Proteins/biosynthesis/chemistry MH - Rhodophyta/*genetics/*metabolism MH - Sequence Homology, Amino Acid EDAT- 1997/01/01 00:00 MHDA- 2001/03/28 10:01 CRDT- 1997/01/01 00:00 PHST- 1997/01/01 00:00 [pubmed] PHST- 2001/03/28 10:01 [medline] PHST- 1997/01/01 00:00 [entrez] AID - 10.1023/a:1005715528297 [doi] PST - ppublish SO - Plant Mol Biol. 1997 Jan;33(1):157-67. doi: 10.1023/a:1005715528297.