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TitleStructural insights into the functions of Raf1 and Bsd2 in hexadecameric Rubisco assembly.
Journal, issue, pagesMol Plant, Vol. 16, Issue 12, Page 1927-1936, Year 2023
Publish dateDec 4, 2023
AuthorsRan Wang / Hui Song / Wenjuan Zhang / Ning Wang / Shijia Zhang / Ruiqi Shao / Cuimin Liu /
PubMed AbstractHexadecameric form I Rubisco, which consisting consists of eight large (RbcL) and eight small (RbcS) subunits, is the most abundant enzyme on earth. Extensive efforts to engineer an improved Rubisco ...Hexadecameric form I Rubisco, which consisting consists of eight large (RbcL) and eight small (RbcS) subunits, is the most abundant enzyme on earth. Extensive efforts to engineer an improved Rubisco to speed up its catalytic efficiency and ultimately increase agricultural productivity. However, difficulties with correct folding and assembly in foreign hosts or in vitro have hampered the genetic manipulation of hexadecameric Rubisco. In this study, we reconstituted Synechococcus sp. PCC6301 Rubisco in vitro using the chaperonin system and assembly factors from cyanobacteria and Arabidopsis thaliana (At). Rubisco holoenzyme was produced in the presence of cyanobacterial Rubisco accumulation factor 1 (Raf1) alone or both AtRaf1 and bundle-sheath defective-2 (AtBsd2) from Arabidopsis. RbcL released from GroEL is assembly capable in the presence of ATP, and AtBsd2 functions downstream of AtRaf1. Cryo-EM structures of RbcL-AtRaf1, RbcL-AtRaf1-AtBsd2, and RbcL revealed that the interactions between RbcL and AtRaf1 are looser than those between prokaryotic RbcL and Raf1, with AtRaf1 tilting 7° farther away from RbcL. AtBsd2 stabilizes the flexible regions of RbcL, including the N and C termini, the 60s loop, and loop 6. Using these data, combined with previous findings, we propose the possible biogenesis pathways of prokaryotic and eukaryotic Rubisco.
External linksMol Plant / PubMed:37853692
MethodsEM (single particle)
Resolution2.9 - 4.1 Å
Structure data

35532

8ilb

EMDB-35532, PDB-8ilb:
The complexes of RbcL, AtRaf1 and AtBSD2 (LFB)
Method: EM (single particle) / Resolution: 3.0 Å

35536

8ilm

EMDB-35536, PDB-8ilm:
The cryo-EM structure of eight Rubisco large subunits (RbcL), two Arabidopsis thaliana Rubisco accumulation factors 1 (AtRaf1), and seven Arabidopsis thaliana Bundle Sheath Defective 2 (AtBSD2)
Method: EM (single particle) / Resolution: 3.3 Å

35605

8io2

EMDB-35605, PDB-8io2:
The Rubisco assembly intermidate of Arabidopsis thaliana Rubisco accumulation factor 1 (AtRaf1) and Rubisco large subunit (RbcL)
Method: EM (single particle) / Resolution: 3.1 Å

35620

8ioj

EMDB-35620, PDB-8ioj:
The Rubisco assembly intermidiate of Rubisco large subunit (RbcL) and Arabidopsis thaliana Rubisco accumulation factor 1 (AtRaf1)
Method: EM (single particle) / Resolution: 4.1 Å

35621

8iol

EMDB-35621, PDB-8iol:
The complex of Rubisco large subunit (RbcL)
Method: EM (single particle) / Resolution: 2.9 Å

Source
  • arabidopsis thaliana (thale cress)
  • synechococcus elongatus pcc 6301 (bacteria)
  • synechococcus sp. (strain atcc 27144 / pcc 6301 / saug 1402/1) (bacteria)
KeywordsLYASE/CHAPERONE / RUBISCO ASSEMBL INTERMIDATES / COMPLEX / CHAPERONE / LYASE-CHAPERONE complex / BIOSYNTHETIC PROTEIN / LYASE / Rubisco assembly intermediate / Rubisco assembly intermidiate / Rubisco large subunit / PHOTOSYNTHESIS

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