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

E3 Ubiquitin Ligase SPL2 Is a Lanthanide-Binding Protein.

International journal of molecular sciences - 27 May 2021

Tracz Michał, Górniak Ireneusz, Szczepaniak Andrzej, Białek Wojciech

Abstract excerpt

The SPL2 protein is an E3 ubiquitin ligase of unknown function. It is one of only three types of E3 ligases found in the outer membrane of plant chloroplasts. In this study, we show that the cytosolic fragment of SPL2 binds lanthanide ions, as evidenced by fluorescence measurements and circular dichroism spectroscopy. We also report that SPL2 undergoes conformational changes upon binding of both Ca2+ and La3+, as...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Binding Sites
Share to Calcium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carrier Proteins

Share to Protein Conformation

Share to Spectrum Analysis

Share to Ubiquitin-Protein Ligases

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 34071935
DOI: 10.3390/ijms22115712
PMCID: PMC8198723

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

E3 Ubiquitin Ligase SPL2 Is a Lanthanide-Binding Protein.PMID 34071935Read ↗

Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis.Semantic proximity Read ↗

EGY3: homologue of S2P protease located in chloroplasts.Semantic proximity Read ↗

LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis in Arabidopsis thaliana.Semantic proximity Read ↗

Altered levels of LIL3 isoforms in Arabidopsis lead to disturbed pigment-protein assembly and chlorophyll synthesis, chlorotic phenotype and impaired photosynthetic performance.Semantic proximity Read ↗

LIL3, a light-harvesting-like protein, plays an essential role in chlorophyll and tocopherol biosynthesis.Semantic proximity Read ↗

Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center.Semantic proximity Read ↗

Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis.Semantic proximity Read ↗

Degradation of the main Photosystem II light-harvesting complex.Semantic proximity Read ↗

Removal of the N-linked glycan structure from the peanut peroxidase prxPNC2: influence on protein stability and activity.Semantic proximity Read ↗

Characterization of the LI818 polypeptide from the green unicellular alga Chlamydomonas reinhardtii.Semantic proximity Read ↗

Functional analysis of light-harvesting-like protein 3 (LIL3) and its light-harvesting chlorophyll-binding motif in Arabidopsis.Semantic proximity Read ↗

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

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