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

The proteolysis adaptor, NblA, is essential for degradation of the core pigment of the cyanobacterial light-harvesting complex.

The Plant journal : for cell and molecular biology - 1 Sept 2015

Sendersky Eleonora, Kozer Noga, Levi Mali, Moizik Michael, Garini Yuval, Shav-Tal Yaron, Schwarz Rakefet

Abstract excerpt

The cyanobacterial light-harvesting complex, the phycobilisome, is degraded under nutrient limitation, allowing the cell to adjust light absorbance to its metabolic capacity. This large light-harvesting antenna comprises a core complex of the pigment allophycocyanin, and rod-shaped pigment assemblies emanating from the core. NblA, a low-molecular-weight protein, is essential for degradation of the phycobilisome....

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Light-Harvesting Protein Complexes

Share to Mutation

Share to Phycobilisomes

Share to Phycocyanin

Share to Synechococcus

Source

Identifiers

PMID: 26173720
DOI: 10.1111/tpj.12931

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

The proteolysis adaptor, NblA, is essential for degradation of the core pigment of the cyanobacterial light-harvesting complex.PMID 26173720Read ↗

Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria.Semantic proximity Read ↗

NblA, a key protein of phycobilisome degradation, interacts with ClpC, a HSP100 chaperone partner of a cyanobacterial Clp protease.Semantic proximity Read ↗

A polypeptide with similarity to phycocyanin alpha-subunit phycocyanobilin lyase involved in degradation of phycobilisomes.Semantic proximity Read ↗

NblA is essential for phycobilisome degradation in Anabaena sp. strain PCC 7120 but not for development of functional heterocysts.Semantic proximity Read ↗

The phycobilisome, a light-harvesting complex responsive to environmental conditions.Semantic proximity Read ↗

A model for early events in the assembly pathway of cyanobacterial phycobilisomes.Semantic proximity Read ↗

Characterization of Synechocystis sp. strain PCC 6803 and deltanbl mutants under nitrogen-deficient conditions.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 ↗

Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

Alanine dehydrogenase activity is required for adequate progression of phycobilisome degradation during nitrogen starvation in Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

NblR is a novel one-component response regulator in the cyanobacterium Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

Small Cab-like proteins retard degradation of photosystem II-associated chlorophyll in Synechocystis sp. PCC 6803: kinetic analysis of pigment labeling with 15N and 13C.Semantic proximity Read ↗

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