Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain

Furukawa, Yoshiaki; Lim, Carolyn; Tosha, Takehiko; Yoshida, Koki; Hagai, Tomoaki; Akiyama, Shuji; Watanabe, Shôji; Nakagome, Kenta; Shiro, Yoshitsugu

doi:10.1371/journal.pone.0204355

Cited by 17 publications

(12 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…6c–h). MDF1 is a conserved eukaryotic β -strand-rich protein and, although structures of the human and Plasmodium falciparum homologues have been determined 19–21 , their functional role has so far remained elusive. MDF1 is located in the E-site of the small ribosomal subunit, where it stabilizes a rotated and swivelled conformation (Figs.…”

mentioning

confidence: 99%

Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome

et al. 2019

View full text Add to dashboard Cite

Microsporidia are eukaryotic parasites that infect essentially all animal species, including many of agricultural importance 1-3 , and are significant opportunistic parasites of humans 4. They are characterized by having a specialized infection apparatus, an obligate intracellular lifestyle 5 , rudimentary mitochondria and the smallest known eukaryotic genomes 5-7. Extreme genome compaction led to minimal gene sizes affecting even conserved ancient complexes such as the ribosome 8-10. In the present study, the cryo-electron microscopy structure of the ribosome from the microsporidium Vairimorpha necatrix is presented, which illustrates how genome compaction has resulted in the smallest known eukaryotic cytoplasmic ribosome. Selection pressure led to the loss of two ribosomal proteins and removal of essentially all eukaryote-specific ribosomal RNA (rRNA) expansion segments, reducing the rRNA to a functionally conserved core. The structure highlights how one microsporidia-specific and several repurposed existing ribosomal proteins compensate for the extensive rRNA reduction. The microsporidian ribosome is kept in an inactive state by two previously uncharacterized dormancy factors that specifically target the functionally important E-site, P-site and polypeptide exit tunnel. The present study illustrates the distinct effects of evolutionary pressure on RNA and protein-coding genes, provides a mechanism for ribosome inhibition and can serve as a structural basis for the development of inhibitors against microsporidian parasites. Reprints and permissions information is available at www.nature.com/reprints.

show abstract

mentioning

confidence: 99%

Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome

et al. 2019

View full text Add to dashboard Cite

show abstract

“…There are 53 up-regulated or uniquely expressed proteins in MDR strains, which are involved in lipid metabolism ( Jang et al., 2008 ; Gu et al., 2019 ), amino acid metabolism ( Stancik et al., 2002 ; Bezsudnova et al., 2017 ), TCA cycle ( Corregido et al., 2019 ), purine anabolic metabolism ( Spurr et al., 2012 ), pyruvate metabolism ( Song et al., 2010 ), fatty acid metabolism ( Nishimaki-Mogami et al., 1987 ), intracellular electron transfer of bacteria ( López Rivero et al., 2019 ), nutrition and energy acquisition ( Drewke et al., 1996 ), and other metabolic processes. In addition, the heavy metal associated (HMA) domain protein which is closely related to the utilization and metabolism of metal ions such as copper ions and zinc ions ( Furukawa et al., 2018 ) is also up-regulated.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analyses of Acinetobacter baumannii Clinical Isolates to Identify Drug Resistant Mechanism

Wang

et al. 2021

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Acinetobacter baumannii is one of the main causes of nosocomial infections. Increasing numbers of multidrug-resistant Acinetobacter baumannii cases have been reported in recent years, but its antibiotic resistance mechanism remains unclear. We studied 9 multidrug-resistant (MDR) and 10 drug-susceptible Acinetobacter baumannii clinical isolates using Label free, TMT labeling approach and glycoproteomics analysis to identify proteins related to drug resistance. Our results showed that 164 proteins exhibited different expressions between MDR and drug-susceptible isolates. These differential proteins can be classified into six groups: a. proteins related to antibiotic resistance, b. membrane proteins, membrane transporters and proteins related to membrane formation, c. Stress response-related proteins, d. proteins related to gene expression and protein translation, e. metabolism-related proteins, f. proteins with unknown function or other functions containing biofilm formation and virulence. In addition, we verified seven proteins at the transcription level in eight clinical isolates by using quantitative RT-PCR. Results showed that four of the selected proteins have positive correlations with the protein level. This study provided an insight into the mechanism of antibiotic resistance of multidrug-resistant Acinetobacter baumannii.

show abstract

“…Human C1orf123 is proposed as one of the human O-GlcNAc transferase interactors, playing a potential role in post-translation modification [ 64 ]. C1orf123 was found to be a novel zinc-binding protein [ 65 , 66 ] that could play a role in mitochondrial oxidative phosphorylation [ 66 ] and could interact specifically with the heavy metal-associated domain of a copper chaperone for superoxide dismutase [ 65 ].…”

Section: Discussionmentioning

confidence: 99%

New Proteins Contributing to Immune Cell Infiltration and Pannus Formation of Synovial Membrane from Arthritis Diseases

Seny

Baiwir

Bianchi

et al. 2021

IJMS

View full text Add to dashboard Cite

An inflamed synovial membrane plays a major role in joint destruction and is characterized by immune cells infiltration and fibroblast proliferation. This proteomic study considers the inflammatory process at the molecular level by analyzing synovial biopsies presenting a histological inflammatory continuum throughout different arthritis joint diseases. Knee synovial biopsies were obtained from osteoarthritis (OA; n = 9), chronic pyrophosphate arthropathy (CPPA; n = 7) or rheumatoid arthritis (RA; n = 8) patients. The histological inflammatory score was determined using a semi-quantitative scale based on synovial hyperplasia, lymphocytes, plasmocytes, neutrophils and macrophages infiltration. Proteomic analysis was performed by liquid chromatography-mass spectrometry (LC-MS/MS). Differentially expressed proteins were confirmed by immunohistochemistry. Out of the 1871 proteins identified and quantified by LC-MS/MS, 10 proteins (LAP3, MANF, LCP1, CTSZ, PTPRC, DNAJB11, EML4, SCARA5, EIF3K, C1orf123) were differentially expressed in the synovial membrane of at least one of the three disease groups (RA, OA and CPPA). Significant increased expression of the seven first proteins was detected in RA and correlated to the histological inflammatory score. Proteomics is therefore a powerful tool that provides a molecular pattern to the classical histology usually applied for synovitis characterization. Except for LCP1, CTSZ and PTPRC, all proteins have never been described in human synovitis.

show abstract

Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain

Cited by 17 publications

References 37 publications

Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome

Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome

Proteomic Analyses of Acinetobacter baumannii Clinical Isolates to Identify Drug Resistant Mechanism

New Proteins Contributing to Immune Cell Infiltration and Pannus Formation of Synovial Membrane from Arthritis Diseases

Contact Info

Product

Resources

About