PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
He, S.* ; Chou, H.T.* ; Matthies, D.* ; Wunder, T.* ; Meyer, M.T.* ; Atkinson, N.* ; Martinez-Sanchez, A.* ; Jeffrey, P.D.* ; Port, S.A.* ; Patena, W.* ; He, G.* ; Chen, V.K.* ; Hughson, F.M.* ; McCormick, A.J.* ; Mueller-Cajar, O.* ; Engel, B.D. ; Yu, Z.* ; Jonikas, M.C.*

The structural basis of Rubisco phase separation in the pyrenoid.

Nat. Plants 6, 1480–1490 (2020)
Postprint DOI PMC
Open Access Green
Approximately one-third of global CO2 fixation occurs in a phase-separated algal organelle called the pyrenoid. The existing data suggest that the pyrenoid forms by the phase separation of the CO2-fixing enzyme Rubisco with a linker protein; however, the molecular interactions underlying this phase separation remain unknown. Here we present the structural basis of the interactions between Rubisco and its intrinsically disordered linker protein Essential Pyrenoid Component 1 (EPYC1) in the model alga Chlamydomonas reinhardtii. We find that EPYC1 consists of five evenly spaced Rubisco-binding regions that share sequence similarity. Single-particle cryo-electron microscopy of these regions in complex with Rubisco indicates that each Rubisco holoenzyme has eight binding sites for EPYC1, one on each Rubisco small subunit. Interface mutations disrupt binding, phase separation and pyrenoid formation. Cryo-electron tomography supports a model in which EPYC1 and Rubisco form a codependent multivalent network of specific low-affinity bonds, giving the matrix liquid-like properties. Our results advance the structural and functional understanding of the phase separation underlying the pyrenoid, an organelle that plays a fundamental role in the global carbon cycle.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
13.256
3.255
10
31
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Co2-concentrating Mechanisms; Small-subunit; Chlamydomonas; Co2; Photosynthesis; Expression; Proteins; Enzymes; System; Gene
Sprache englisch
Veröffentlichungsjahr 2020
HGF-Berichtsjahr 2020
ISSN (print) / ISBN 2055-026X
e-ISSN 2055-0278
Zeitschrift Nature Plants
Quellenangaben Band: 6, Heft: , Seiten: 1480–1490 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus Peer reviewed
Institut(e) Helmholtz Pioneer Campus (HPC)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Pioneer Campus
PSP-Element(e) G-510008-001
Förderungen Howard Hughes Medical Institute
DOI 10.1038/s41477-020-00811-y
WOS ID WOS:000591958700001
Scopus ID 85096437474
PubMed ID 33230314
Erfassungsdatum 2020-11-30
[➜Korrektur melden]