Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
ROLE OF PSII-L PROTEIN (PSBL GENE-PRODUCT) ON THE ELECTRON-TRANSFER IN PHOTOSYSTEM-II COMPLEX .1. OVER-PRODUCTION OF WILD-TYPE AND MUTANT VERSIONS OF PSII-L PROTEIN AND RECONSTITUTION INTO THE PSII CORE COMPLEX
Autore:
OZAWA S; KOBAYASHI T; SUGIYAMA R; HOSHIDA H; SHIINA T; TOYOSHIMA Y;
Indirizzi:
KYOTO UNIV,GRAD SCH HUMAN & ENVIRONM STUDIES,SAKYO KU,YOSHIDA NIHONMATU CHO KYOTO 60601 JAPAN KYOTO UNIV,GRAD SCH HUMAN & ENVIRONM STUDIES,SAKYO KU KYOTO 60601 JAPAN
Titolo Testata:
Plant molecular biology
fascicolo: 1, volume: 34, anno: 1997,
pagine: 151 - 161
SICI:
0167-4412(1997)34:1<151:ROPP(G>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRIMARY QUINONE ACCEPTOR; MOLECULAR-MASS PROTEINS; NUCLEOTIDE-SEQUENCE; CHLOROPLAST GENOME; ESCHERICHIA-COLI; REACTION CENTERS; ORGANIZATION; B-559; QA;
Keywords:
PSII-L; OVER PRODUCTION; PHOTOSYSTEM II; PSBL; Q(A); RECONSTITUTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
S. Ozawa et al., "ROLE OF PSII-L PROTEIN (PSBL GENE-PRODUCT) ON THE ELECTRON-TRANSFER IN PHOTOSYSTEM-II COMPLEX .1. OVER-PRODUCTION OF WILD-TYPE AND MUTANT VERSIONS OF PSII-L PROTEIN AND RECONSTITUTION INTO THE PSII CORE COMPLEX", Plant molecular biology, 34(1), 1997, pp. 151-161

Abstract

To establish a system for over-production of PSII-L protein which is a component of photosystem II (PSII) complex, a plasmid designated as pMAL-psbL was constructed and expressed in Escherichia coli JM109. A fusion protein of PSII-L and maltose-binding proteins (53 kDa on SDS-PAGE) was accumulated in E. coli cells to a level of 10% of the total protein upon isopropyl-beta-D-thiogalactopyranoside (IPTG) induction. The carboxyl-terminal part of 5.0 kDa was cleaved from the fusion protein and purified by an anion exchange column chromatography in the presence of detergents. This 5.0 kDa protein was identified as PSII-L by amino-terminal amino acid sequence analysis and the chromatographic behavior on an anion exchange gel. A few types of mutant PSII-L were also prepared by the essentially same procedure except for using plasmids which contain given mutations in psbL gene. Plastoquinone-9 (PQ-9) depleted PSII reaction center core complex consisting of D1, D2, CP47, cytochrome b-559 (cyt b-559), PSII-I and PSII-W was reconstituted with PQ-9 and digalactosyldiglyceride (DGDG) together with the wild-type or mutant PSII-L produced in E. coli or isolated PSII-L from spinach. Significant difference between the wild-type PSII-L proteins from E. coli and spinach was not recognized in the effectiveness to recover the photoinduced electron transfer activity in the resulting complexes. The analysis of stoichiometry of PQ-9 per reaction center in the PQ-9 reconstituted PS II revealed that two molecules of PQ-9 were reinserted into a reaction center independent of the presence or absence of PSII-L. These results suggest that PSII-L recovers the electron transfer activity in the reconstituted RC by a mechanism different from the stabilization of PQ-9 in the QA Site of PSII. Ubiquinone-10 (UQ-10), but not plastoquinone-2 (PQ-2), substituted PQ-9 for recovering the PSII-L supported electron transfer activity in the reconstituted PSII reaction center complexes. The results obtained with the mutant PSII-L proteins revealed that the carboxyl terminal part rather than amino terminal part of PSII-L is crucial for recovering the electron transfer activity in the reconstituted complexes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 08:58:38