scholarly journals Faculty Opinions recommendation of Characterization of the nuclear export adaptor protein Nmd3 in association with the 60S ribosomal subunit.

2012 ◽  
Author(s):  
Susan Gerbi
Keyword(s):  
Nuclear Export ◽  
Ribosomal Subunit ◽  
Adaptor Protein

scholarly journals Characterization of the nuclear export adaptor protein Nmd3 in association with the 60S ribosomal subunit

2010 ◽  
Vol 189 (7) ◽  
pp. 1079-1086 ◽  
Author(s):  
Jayati Sengupta ◽  
Cyril Bussiere ◽  
Jesper Pallesen ◽  
Matthew West ◽  
Arlen W. Johnson ◽  
...  
Keyword(s):  
Binding Site ◽  
Nuclear Export ◽  
Large Subunit ◽  
Ribosomal Subunit ◽  
Adaptor Protein ◽  
Structural Data ◽  
Release Mechanism ◽  
Nuclear Pore ◽  
Subunit Joining

The nucleocytoplasmic shuttling protein Nmd3 is an adaptor for export of the 60S ribosomal subunit from the nucleus. Nmd3 binds to nascent 60S subunits in the nucleus and recruits the export receptor Crm1 to facilitate passage through the nuclear pore complex. In this study, we present a cryoelectron microscopy (cryo-EM) reconstruction of the 60S subunit in complex with Nmd3 from Saccharomyces cerevisiae. The density corresponding to Nmd3 is directly visible in the cryo-EM map and is attached to the regions around helices 38, 69, and 95 of the 25S ribosomal RNA (rRNA), the helix 95 region being adjacent to the protein Rpl10. We identify the intersubunit side of the large subunit as the binding site for Nmd3. rRNA protection experiments corroborate the structural data. Furthermore, Nmd3 binding to 60S subunits is blocked in 80S ribosomes, which is consistent with the assigned binding site on the subunit joining face. This cryo-EM map is a first step toward a molecular understanding of the functional role and release mechanism of Nmd3.

scholarly journals A nuclear role for the DEAD-box protein Dbp5 in tRNA export

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Azra Lari ◽  
Arvind Arul Nambi Rajan ◽  
Rima Sandhu ◽  
Taylor Reiter ◽  
Rachel Montpetit ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Ribosomal Subunit ◽  
Nucleocytoplasmic Transport ◽  
Alanine Scanning Mutagenesis ◽  
Dead Box ◽  
Nuclear Shuttling ◽  
Export Signal

Dbp5 is an essential DEAD-box protein that mediates nuclear mRNP export. Dbp5 also shuttles between nuclear and cytoplasmic compartments with reported roles in transcription, ribosomal subunit export, and translation; however, the mechanism(s) by which nucleocytoplasmic transport occurs and how Dbp5 specifically contributes to each of these processes remains unclear. Towards understanding the functions and transport of Dbp5 in Saccharomyces cerevisiae, alanine scanning mutagenesis was used to generate point mutants at all possible residues within a GFP-Dbp5 reporter. Characterization of the 456 viable mutants led to the identification of an N-terminal Xpo1-dependent nuclear export signal in Dbp5, in addition to other separation-of-function alleles, which together provide evidence that Dbp5 nuclear shuttling is not essential for mRNP export. Rather, disruptions in Dbp5 nucleocytoplasmic transport result in tRNA export defects, including changes in tRNA shuttling dynamics during recovery from nutrient stress.

Characterization of putative salinity-responsive biomarkers in olive (Olea europaea L.)

2021 ◽  
pp. 1-11
Author(s):  
Monther T. Sadder ◽  
Ahmad F. Ateyyeh ◽  
Hodayfah Alswalmah ◽  
Adel M. Zakri ◽  
Abdullah A. Alsadon ◽  
...  
Keyword(s):  
Food Production ◽  
Stress Protein ◽  
Adaptor Protein ◽  
Structural Features ◽  
Nacl Stress ◽  
Soil Salinization ◽  
Limiting Factors ◽  
Stress Levels ◽  
Quality Water

Abstract Low-quality water and soil salinization are increasingly becoming limiting factors for food production, including olive – a major fruit crop in several parts of the world. Identifying putative salinity-stress tolerance in olive would be helpful in the future development of new tolerant varieties. In this study, novel salinity-responsive biomarkers (SRBs) were characterized in the species, namely, monooxygenase 1 (OeMO1), cation calcium exchanger 1 (OeCCX1), salt tolerance protein (OeSTO), proteolipid membrane potential modulator (OePMP3), universal stress protein (OeUSP2), adaptor protein complex 4 medium mu4 subunit (OeAP-4), WRKY1 transcription factor (OeWRKY1) and potassium transporter 2 (OeKT2). Unique structural features were highlighted for encoded proteins as compared with other plant homologues. The expression of olive SRBs was investigated in leaves of young plantlets of two cultivars, ‘Nabali’ (moderately tolerant) and ‘Picual’ (tolerant). At 60 mM NaCl stress level, OeMO1, OeSTO, OePMP3, OeUSP2, OeAP-4 and OeWRKY1 were up-regulated in ‘Nabali’ as compared with ‘Picual’. On the other hand, OeCCX1 and OeKT2 were up-regulated at three stress levels (30, 60 and 90 mM NaCl) in ‘Picual’ as compared to ‘Nabali’. Salinity tolerance in olive presumably engages multiple sets of responsive genes triggered by different stress levels.

scholarly journals Mapping the Functional Domains of Yeast NMD3, the Nuclear Export Adapter for the 60 S Ribosomal Subunit

2006 ◽  
Vol 281 (48) ◽  
pp. 36579-36587 ◽  
Author(s):  
John Hedges ◽  
Yen-I Chen ◽  
Matthew West ◽  
Cyril Bussiere ◽  
Arlen W. Johnson
Keyword(s):  
Nuclear Export ◽  
Ribosomal Subunit ◽  
Functional Domains

scholarly journals Rrs1p, a ribosomal protein L11-binding protein, is required for nuclear export of the 60S pre-ribosomal subunit inSaccharomyces cerevisiae

FEBS Letters ◽  
2004 ◽  
Vol 565 (1-3) ◽  
pp. 106-110 ◽  
Author(s):  
Keita Miyoshi ◽  
Chiharu Shirai ◽  
Chihiro Horigome ◽  
Kazuhiko Takenami ◽  
Junko Kawasaki ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Nuclear Export ◽  
Binding Protein ◽  
Ribosomal Subunit ◽  
Ribosomal Protein L11

scholarly journals New Bone Marrow Failure Genes: DNAJC21 and ERCC6L2

Blood ◽  
2017 ◽  
Vol 130 (Suppl_1) ◽  
pp. SCI-22-SCI-22
Author(s):  
Inderjeet Dokal
Keyword(s):  
Bone Marrow ◽  
Dna Damage ◽  
Nuclear Export ◽  
Conflicts Of Interest ◽  
Excision Repair ◽  
Bone Marrow Failure ◽  
Retinal Dystrophy ◽  
Ribosomal Subunit ◽  
Genotoxic Stress ◽  
Biallelic Mutations

A significant number of cases with bone marrow failure present with one or more extra-hematopoietic abnormality. This suggests a constitutional or genetic basis, and yet many of them remain uncharacterized. Through exome sequencing, we have recently identified two sub groups of these cases, one defined by germline biallelic mutations in DNAJC21 (DNAJ homolog subfamily C member 21) and the other in ERCC6L2 (excision repair cross complementing 6 like-2). Patients with DNAJC21 mutations are characterized by global bone marrow failure in early childhood. They can also have a variable number of extra-hematopoietic abnormalities such as short stature and retinal dystrophy. The encoded protein associates with ribosomal RNA (rRNA) and plays a highly conserved role in the maturation of the 60S ribosomal subunit. Lymphoblastoid patient cells exhibit increased sensitivity to the transcriptional inhibitor actinomycin D and reduced levels of rRNA. Characterisation of mutations has revealed impairment in interactions with cofactors (PA2G4, HSPA8 and ZNF622) involved in 60S maturation. DNAJC21 deficiency results in cytoplasmic accumulation of the 60S nuclear export factor PA2G4, aberrant ribosome profiles and increased cell death. Collectively these findings demonstrate that biallelic mutations in DNAJC21 cause disease due to defects in early nuclear rRNA biogenesis and late cytoplasmic maturation of the 60S subunit. Patients harbouring biallelic ERCC6L 2 mutations are characterized by bone marrow failure (in childhood or early adulthood) and one or more extra-hematopoietic abnormality such as microcephaly. Knockdown of ERCC6L2 in human cells significantly reduces their viability upon exposure to the DNA damaging agent irofulven but not etoposide and camptothecin suggesting a role in nucleotide excision repair. ERCC6L2 knockdown cells and patient cells harbouring biallelic ERCC6L2 mutations also display H2AX phosphorylation that significantly increases upon genotoxic stress, suggesting an early DNA damage response. ERCC6L2 is seen to translocate to mitochondria as well as the nucleus in response to DNA damage and its knockdown induces intracellular reactive oxygen species (ROS). Treatment with the ROS scavenger, N-acetyl-cysteine, attenuates the irofulven-induced cytotoxicity in ERCC6L2 knockdown cells and abolishes its traffic to mitochondria and nucleus in response to this DNA damaging agent. Collectively, these observations suggest that ERCC6L2has a pivotal rolein DNA repair and mitochondrial function. In conclusion, ERCC6L2 and DNAJC21 have an important role in maintaining genomic stability and ribosome biogenesis, respectively. They bring into focus new biological connections/pathways whose constitutional disruption is associated with defective hematopoiesis since patients harbouring germline biallelic mutations in these genes uniformly have bone marrow failure. Disclosures No relevant conflicts of interest to declare.

Requirements for the nuclear export of the small ribosomal subunit

2002 ◽  
Vol 115 (14) ◽  
pp. 2985-2995 ◽  
Author(s):  
Terence I. Moy ◽  
Pamela A. Silver
Keyword(s):  
Nuclear Export ◽  
Ribosome Biogenesis ◽  
Large Scale ◽  
Ribosomal Subunit ◽  
Small Subunit ◽  
Temperature Sensitive ◽  
Yeast Saccharomyces Cerevisiae ◽  
Small Ribosomal Subunit ◽  
Factors Affecting ◽  
The Stability

Eukaryotic ribosome biogenesis requires multiple steps of nuclear transport because ribosomes are assembled in the nucleus while protein synthesis occurs in the cytoplasm. Using an in situ RNA localization assay in the yeast Saccharomyces cerevisiae, we determined that efficient nuclear export of the small ribosomal subunit requires Yrb2, a factor involved in Crm1-mediated export. Furthermore, in cells lacking YRB2, the stability and abundance of the small ribosomal subunit is decreased in comparison with the large ribosomal subunit. To identify additional factors affecting small subunit export, we performed a large-scale screen of temperature-sensitive mutants. We isolated new alleles of several nucleoporins and Ran-GTPase regulators. Together with further analysis of existing mutants,we show that nucleoporins previously shown to be defective in ribosomal assembly are also defective in export of the small ribosomal subunit.

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