Biomaterial Database

N-proximal sequence motif in light-harvesting chlorophyll a/b-binding protein is essential for the trimerization of light-harvesting chlorophyll a/b complex. 1995

S Hobe, and R Förster, and J Klingler, and H Paulsen

Botanisches Institut III der Universität, München, Germany.

The major light-harvesting complex (LHCII) of photosystem II can be reconstituted in its native, trimeric form starting from its apoprotein light-harvesting chlorophyll a/b-binding protein (LHCP), pigments, and thylakoid lipids. In this paper we identify segments in the LHCP polypeptide that are essential for the formation of stable LHCII trimers by analyzing N- and C-terminal deletion mutants of LHCP and mutants carrying point-specific amino acid exchanges. C-terminal deletions that do not abolish pigment binding to LHCP do not affect trimerization either. By contrast, on the N-terminus of LHCP, where as many as 61 amino acids can be deleted without significant effects on pigment binding, only 15 amino acids are dispensible for LHCII trimer formation. This indicates that structural elements between amino acids 16 and 61 are involved in the stabilization of LHCII trimers but not monomers. Closer inspection of this protein domain in a more detailed mutation analysis revealed that amino acids W16 and/or Y17 as well as R21 are essential for the formation of LHCII trimers. These amino acids are conserved in virtually all known sequences of LHCII apoproteins but only in some of the minor chlorophyll a/b complexes. Possible functions of the crucial residues are discussed.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011489	Protein Denaturation	Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.	Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D004591	Electrophoresis, Polyacrylamide Gel	Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.	Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001483	Base Sequence	The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.	DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D001704	Biopolymers	Polymers synthesized by living organisms. They play a role in the formation of macromolecular structures and are synthesized via the covalent linkage of biological molecules, especially AMINO ACIDS; NUCLEOTIDES; and CARBOHYDRATES.	Bioplastics,Bioplastic,Biopolymer
D016296	Mutagenesis	Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.	Mutageneses
D045322	Photosynthetic Reaction Center Complex Proteins	Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.	Photosynthetic Complex,Photosynthetic Reaction Center,Photosynthetic Reaction Center Complex Protein,Photosynthetic Complexes,Photosynthetic Reaction Centers,Center, Photosynthetic Reaction,Complex, Photosynthetic,Complexes, Photosynthetic,Reaction Center, Photosynthetic,Reaction Centers, Photosynthetic
D045332	Photosystem II Protein Complex	A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN.	Chloroplast Reaction Center Protein D1,D1 Photosystem II Protein, Plant,Light-Induced D1 Protein, Photosystem II,Oxygen Evolving Enzyme,PRCP II D2 Protein,Photosystem II,Photosystem II Reaction Center,Photosystem II Reaction Center Complex D1 Protein,Photosystem II Reaction Center Complex D2 Protein,RCII-D1 Protein,Water Oxidase,Water-Splitting Enzyme of Photosynthesis,Enzyme, Oxygen Evolving,Evolving Enzyme, Oxygen,Light Induced D1 Protein, Photosystem II,Oxidase, Water,Photosynthesis Water-Splitting Enzyme,Water Splitting Enzyme of Photosynthesis
D045342	Light-Harvesting Protein Complexes	Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX.	Antenna Complexes, Light-Harvesting,Light-Harvesting Antenna Complexes,Light-Harvesting Chlorophyll Protein,Light-Harvesting Chlorophyll Protein Complexes,Antenna Complexes, Light Harvesting,Chlorophyll Protein, Light-Harvesting,Complexes, Light-Harvesting Antenna,Complexes, Light-Harvesting Protein,Light Harvesting Antenna Complexes,Light Harvesting Chlorophyll Protein,Light Harvesting Chlorophyll Protein Complexes,Light Harvesting Protein Complexes,Protein Complexes, Light-Harvesting