A look within LHCII: Differential analysis of the Lhcbl-3 complexes building the major trimeric antenna complex of higher-plant photosynthesis

被引:123
作者
Caffarri, S
Croce, R
Cattivelli, L
Bassi, R
机构
[1] Univ Verona, Dipartimento Sci & Tecnol, I-37134 Verona, Italy
[2] CNR, ITC Ist Biofis, Sez Trento, Povo, Tn, Italy
[3] Univ Aix Marseille 2, LGBP, Fac Sci Luminy, Dept Biol, F-13288 Marseille 09, France
[4] Ist Sperimentale Cerealicoltura, I-29017 Fiorenzuola Darda, PC, Italy
关键词
D O I
10.1021/bi036265i
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The major antenna complex of higher-plant photosynthesis, LHCII, is composed by the products of three genes, namely, Lhcbl-2-3. In this paper, the biochemical and spectroscopic proper-ties of each of the three gene products were investigated. The three complexes were obtained by overexpression of the apoproteins in bacteria and refolding in vitro with purified pigments, thus allowing detection of differences in the structure/function of the pigment-binding gene products. The analyses showed that Lhcb1 and Lhcb2 complexes have similar pigment binding properties, although not identical, while Lhcb3 is clearly different with respect to both pigment binding and spectral properties and cannot produce homotrimers in vitro. Heterotrimers containing Lhcb3 together with Lhcb1 and/or -2 proteins were obtained upon assembly with Lhcb proteins purified from thylakoids. The major functional characteristics of Lhcb3 with respect to Lhcb1 and -2 consisted in (i) a red-shift of one specific chlorophyll a chromophore, strongly affecting the red-most region of the absorption spectrum and (ii) a different specificity for xanthophylls binding to sites L2 and N1. These properties make Lhcb3 a relative sink for excitation energy in isolated heterotrimers with Lhcb1 + Lhcb2, and potentially, a preferential site of regulation of the antenna function in excess light conditions.
引用
收藏
页码:9467 / 9476
页数:10
相关论文
共 55 条
[1]   PROTEIN-PHOSPHORYLATION IN REGULATION OF PHOTOSYNTHESIS [J].
ALLEN, JF .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1098 (03) :275-335
[2]   CHLOROPHYLL-PROTEINS OF 2 PHOTOSYSTEM-I PREPARATIONS FROM MAIZE [J].
BASSI, R ;
MACHOLD, O ;
SIMPSON, D .
CARLSBERG RESEARCH COMMUNICATIONS, 1985, 50 (03) :145-162
[3]   CHANGES IN THE ORGANIZATION OF STROMA MEMBRANES INDUCED BY INVIVO STATE-1-STATE-2 TRANSITION [J].
BASSI, R ;
GIACOMETTI, GM ;
SIMPSON, DJ .
BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 935 (02) :152-165
[4]   LIGHT-HARVESTING CHLOROPHYLL-A/B-PROTEINS (LHCII) POPULATIONS IN PHOSPHORYLATED MEMBRANES [J].
BASSI, R ;
RIGONI, F ;
BARBATO, R ;
GIACOMETTI, GM .
BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 936 (01) :29-38
[5]   A SUPRAMOLECULAR LIGHT-HARVESTING COMPLEX FROM CHLOROPLAST PHOTOSYSTEM-II MEMBRANES [J].
BASSI, R ;
DAINESE, P .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 204 (01) :317-326
[6]   Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes [J].
Boekema, EJ ;
van Roon, H ;
van Breemen, JFL ;
Dekker, JP .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 266 (02) :444-452
[7]   The major antenna complex of photosystem II has a xanthophyll binding site not involved in light harvesting [J].
Caffarri, S ;
Croce, R ;
Breton, J ;
Bassi, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (38) :35924-35933
[8]   Recombinant Lhca2 and Lhca3 subunits of the photosystem I antenna system [J].
Castelletti, S ;
Morosinotto, T ;
Robert, B ;
Caffarri, S ;
Bassi, R ;
Croce, R .
BIOCHEMISTRY, 2003, 42 (14) :4226-4234
[9]   Absorption spectra of chlorophyll a and b in Lhcb protein environment [J].
Cinque, G ;
Croce, R ;
Bassi, R .
PHOTOSYNTHESIS RESEARCH, 2000, 64 (2-3) :233-242
[10]   The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants [J].
Croce, R ;
Remelli, R ;
Varotto, C ;
Breton, J ;
Bassi, R .
FEBS LETTERS, 1999, 456 (01) :1-6