Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Biochemical journal - 30 Oct 2020

Proctor Matthew S, Pazderník Marek, Jackson Philip J, Pilný Jan, Martin Elizabeth C, Dickman Mark J, Canniffe Daniel P, Johnson Matthew P, Hunter C Neil, Sobotka Roman, Hitchcock Andrew

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carbon-Oxygen Ligases
Share to Chlorophyll

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyanobacteria

Share to Light-Harvesting Protein Complexes

Share to Photosystem II Protein Complex

Share to Synechocystis

Share to Xanthophylls

Share to Zeaxanthins

Source

Identifiers

PMID: 32990304
DOI: 10.1042/BCJ20200561

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Xanthophyll carotenoids stabilise the association of cyanobacterial chlorophyll synthase with the LHC-like protein HliD.PMID 32990304Read ↗

Plant LHC-like proteins show robust folding and static non-photochemical quenching.Semantic proximity Read ↗

Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes.Semantic proximity Read ↗

A novel high light-inducible carotenoid-binding protein complex in the thylakoid membranes of Synechocystis PCC 6803.Semantic proximity Read ↗

Inactivation of genes encoding plastoglobuli-like proteins in Synechocystis sp. PCC 6803 leads to a light-sensitive phenotype.Semantic proximity Read ↗

The high light-inducible polypeptides in Synechocystis PCC6803. Expression and function in high light.Semantic proximity Read ↗

Association of High Light-Inducible HliA/HliB Stress Proteins with Photosystem 1 Trimers and Monomers of the Cyanobacterium Synechocystis PCC 6803.Semantic proximity Read ↗

The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria.Semantic proximity Read ↗

1-N-histidine phosphorylation of ChlD by the AAA+ ChlI2 stimulates magnesium chelatase activity in chlorophyll synthesis.Semantic proximity Read ↗

Elevated growth temperature can enhance photosystem I trimer formation and affects xanthophyll biosynthesis in Cyanobacterium Synechocystis sp. PCC6803 cells.Semantic proximity Read ↗

Role of the Longest Arm of Phycobilisome Core-Membrane Linker in Assembling the Phycobilisomes From Synechocystis sp. PCC 6803.Semantic proximity Read ↗

An intermediate membrane subfraction in cyanobacteria is involved in an assembly network for Photosystem II biogenesis.Semantic proximity Read ↗

Involvement of carotenoids in the synthesis and assembly of protein subunits of photosynthetic reaction centers of Synechocystis sp. PCC 6803.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.