This work was supported by the Italian Ministry of Education, University and Research, “Futuro in Ricerca 2013” program RBFR1334SB to CP

A Amunts

A Shevchenko

AE Yakushevska

Angelica Chiodoni

B Andersson

B Daum

B Gobets

B Granvogl

B Hankamer

C Pagliano

Cristina Pagliano

DJ Arnon

EF Pettersen

EJ Boekema

EM Aro

Emilio Marengo

Fabio Gosetti

G Groth

G Jackowski

G Tang

Guido Saracco

H Kirchhoff

J Barber

J Nield

J Standfuss

James Barber

JE Mullet

Jon Nield

Jose Alejandro Muñoz Tabares

JP Dekker

K Ido

K Ifuku

KH Rhee

M Balsera

M Heel van

Marcello Manfredi

O Nanba

PA Albertsson

Pascal Albanese

PW Hemelrijk

R Grondelle van

R Kouřil

R Nevo

S Barera

S Caffarri

S Eshaghi

S Jansson

S Järvi

U Hellmann

UK Laemmli

V Calderone

X Pan

Y Umena

ZF Liu

Photosynthesis Research

In higher plants, photosystem II (PSII) is a multi-subunit pigment-protein complex embedded in the thylakoid membranes of chloroplasts, where it is present mostly in dimeric form within the grana. Its light-harvesting antenna system, LHCII, is composed of trimeric and monomeric complexes, which can associate in variable number with the dimeric PSII core complex in order to form different types of PSII-LHCII supercomplexes. Moreover, PSII-LHCII supercomplexes can laterally associate within the thylakoid membrane plane, thus forming higher molecular mass complexes, termed PSII-LHCII megacomplexes (Boekema et al. 1999a, in Biochemistry 38:2233-2239; Boekema et al. 1999b, in Eur J Biochem 266:444-452). In this study, pure PSII-LHCII megacomplexes were directly isolated from stacked pea thylakoid membranes by a rapid single-step solubilization, using the detergent n-dodecyl-α-D-maltoside, followed by sucrose gradient ultracentrifugation. The megacomplexes were subjected to biochemical and structural analyses. Transmission electron microscopy on negatively stained samples, followed by single-particle analyses, revealed a novel form of PSII-LHCII megacomplexes, as compared to previous studies (Boekema et al.1999a, in Biochemistry 38:2233-2239; Boekema et al. 1999b, in Eur J Biochem 266:444-452), consisting of two PSII-LHCII supercomplexes sitting side-by-side in the membrane plane, sandwiched together with a second copy. This second copy of the megacomplex is most likely derived from the opposite membrane of a granal stack. Two predominant forms of intact sandwiched megacomplexes were observed and termed, according to (Dekker and Boekema 2005 Biochim Biophys Acta 1706:12-39), as (C2S2)4 and (C2S2 + C2S2M2)2 megacomplexes. By applying a gel-based proteomic approach, the protein composition of the isolated megacomplexes was fully characterized. In summary, the new structural forms of isolated megacomplexes and the related modeling performed provide novel insights into how PSII-LHCII supercomplexes may bind to each other, not only in the membrane plane, but also between granal stacks within the chloroplast

Albanese, Pascal

Nield, Jon

Tabares, Jose Alejandro Muñoz

Chiodoni, Angelica

Saracco, Guido

Barber, James

MANFREDI, MARCELLO

GOSETTI, Fabio

MARENGO, Emilio

PAGLIANO, Cristina

Archivio Istituzionale della Ricerca- Università del Piemonte Orientale

Isolation of novel PSII-LHCII megacomplexes from pea plants characterized by a combination of proteomics and electron microscopy

Albanese, P

Nield, J

Tabares, JAM

Chiodoni, A

Manfredi, M

Gosetti, F

Marengo, E

Saracco, G

Barber, J

Pagliano, C

Queen Mary Research Online

ALBANESE, PASCAL

SARACCO, GUIDO

PAGLIANO, CRISTINA

Muñoz Tabares, Jose Alejandro

Manfredi, Marcello

Gosetti, Fabio

Marengo, Emilio

PORTO@iris (Publications Open Repository TOrino - Politecnico di Torino)

Muñoz Tabares, Jose Alejandro

Pagliano, Cristina

PORTO Publications Open Repository TOrino

Crossref

https://qmro.qmul.ac.uk/xmlui/bitstream/handle/123456789/11645/Nield%20Isolation%20of%20novel%20PSII-LHCII%202016%20Accepted.pdf?sequence=1

Isolation of novel PSII-LHCII megacomplexes from pea plants characterized by a combination of proteomics and electron microscopy

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Archivio Istituzionale della Ricerca- Università del Piemonte Orientale

Queen Mary Research Online

PORTO@iris (Publications Open Repository TOrino - Politecnico di Torino)

PORTO Publications Open Repository TOrino

Crossref