Xanthophyll carotenoids stabilise the association of cyanobacterial chlorophyll synthase with the LHC-like protein HliD

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901342" target="_blank" >RIV/60076658:12310/20:43901342 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/20:00535059

Result on the web

<a href="https://portlandpress.com/biochemj/article/477/20/4021/226545/Xanthophyll-carotenoids-stabilise-the-association" target="_blank" >https://portlandpress.com/biochemj/article/477/20/4021/226545/Xanthophyll-carotenoids-stabilise-the-association</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1042/BCJ20200561" target="_blank" >10.1042/BCJ20200561</a>

Result language

angličtina

Original language name

Xanthophyll carotenoids stabilise the association of cyanobacterial chlorophyll synthase with the LHC-like protein HliD

Original language description

Chlorophyll synthase (ChlG) catalyses a terminal reaction in the chlorophyll biosynthesis pathway, attachment of phytol or geranylgeraniol to the C17 propionate of chlorophyllide. Cyanobacterial ChlG forms a stable complex with high light-inducible protein D (HliD), a small single-helix protein homologous to the third transmembrane helix of plant light-harvesting complexes (LHCs). The ChlG-HliD assembly binds chlorophyll, beta-carotene, zeaxanthin and myxoxanthophyll and associates with the YidC insertase, most likely to facilitate incorporation of chlorophyll into translated photosystem apoproteins. HliD independently coordinates chlorophyll and beta-carotene but the role of the xanthophylls, which appear to be exclusive to the core ChlG-HliD assembly, is unclear. Here we generated mutants of Synechocystis sp. PCC 6803 lacking specific combinations of carotenoids or HliD in a background with FLAG- or His-tagged ChlG. Immunoprecipitation experiments and analysis of isolated membranes demonstrate that the absence of zeaxanthin and myxoxanthophyll significantly weakens the interaction between HliD and ChlG. ChlG alone does not bind carotenoids and accumulation of the chlorophyllide substrate in the absence of xanthophylls indicates that activity/stability of the `naked&apos; enzyme is perturbed. In contrast, the interaction of HliD with a second partner, the photosystem II assembly factor Ycf39, is preserved in the absence of xanthophylls. We propose that xanthophylls are required for the stable association of ChlG and HliD, acting as a `molecular glue&apos; at the lateral transmembrane interface between these proteins; roles for zeaxanthin and myxoxanthophyll in ChlG-HliD complexation are discussed, as well as the possible presence of similar complexes between LHC-like proteins and chlorophyll biosynthesis enzymes in plants.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/GX19-29225X" target="_blank" >GX19-29225X: Intertwined biogenesis of photosystems I and II: born together to work together</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochemical Journal

ISSN

0264-6021

e-ISSN

—

Volume of the periodical

477

Issue of the periodical within the volume

20

Country of publishing house

GB - UNITED KINGDOM

Number of pages

16

Pages from-to

4021-4036

UT code for WoS article

000588274400004

EID of the result in the Scopus database

2-s2.0-85094983874