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Structure and mechanism of the Rubisco-assembly chaperone Raf1.

Abstract：

:Biogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of ∼40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL8 complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a β-sheet dimerization domain and a flexibly linked α-helical domain. Chemical cross-linking and EM reconstruction indicate that the β-domains bind along the equator of each RbcL2 unit, and the α-helical domains embrace the top and bottom edges of RbcL2. Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Hauser T,Bhat JY,Miličić G,Wendler P,Hartl FU,Bracher A,Hayer-Hartl M

doi

10.1038/nsmb.3062

subject

Has Abstract

pub_date

2015-09-01 00:00:00

pages

720-8

issue

9

eissn

1545-9993

issn

1545-9985

pii

nsmb.3062

journal_volume

22

pub_type

杂志文章

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