Environmental Regulation of Prions in Yeast

doi:10.1201/b16586-13

Cited by 12 publications

(18 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, recognition of cytosolic proteins for their cognate mRNAs has precedents. For example the survey of RNA binders in S. cerevisiae described above, found that 30% of RNA-binding proteins tested bound their own mRNAs, and many of these proteins were cytosolic (Scherrer et al, 2010). A similar finding was reported in survey of the RNAs bound by known RNA-binding proteins in S. cerevisiae (Hogan et al, 2008).…”

Section: The Cellular Location Of the Sec2p Interaction With Its Mrnasupporting

confidence: 71%

“…To our knowledge, the identification of GEF as an RNA-binding protein is unique among fungi. However, several Arf GTPases have been shown to bind mRNA in S. cerevisiae (Trautwein et al, 2004;Scherrer et al, 2010) and in mammalian cells, Arf-GEF1 was identified as a candidate RNA-binding protein in the Atlas of mRNA-binding proteins (Castello et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles

Caballero-Lima

Hautbergue

Wilson

et al. 2014

Molecular Microbiology

View full text Add to dashboard Cite

Candida albicans hyphae grow in a highly polarized fashion from their tips. This polarized growth requires the continuous delivery of secretory vesicles to the tip region. Vesicle delivery depends on Sec2p, the Guanine Exchange Factor (GEF) for the Rab GTPase Sec4p. GTP bound Sec4p is required for the transit of secretory vesicles from the trans-Golgi to sites of polarized growth. We previously showed that phosphorylation of Sec2p at residue S584 was necessary for Sec2p to support hyphal, but not yeast growth. Here we show that on secretory vesicles SEC2 mRNA is physically associated with Sec2p. Moreover, we show that the phosphorylation of S584 allows SEC2 mRNA to dissociate from Sec2p and we speculate that this is necessary for Sec2p function and/or translation. During hyphal extension, the growing tip may be separated from the nucleus by up to 15 μm. Transport of SEC2 mRNA on secretory vesicles to the tip localizes SEC2 translation to tip allowing a sufficient accumulation of this key protein at the site of polarized growth.

show abstract

Section: The Cellular Location Of the Sec2p Interaction With Its Mrnasupporting

confidence: 71%

Section: Discussionmentioning

confidence: 99%

In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles

Caballero-Lima

Hautbergue

Wilson

et al. 2014

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…These include other preribosomal, polysomal, nucleolar, and translation associated proteins (Figure 2A, Table S3). In addition to their known targets of rRNA, tRNA or snoRNA for ribosome biogenesis, or their role in other cellular functions such as vacuolar trafficking or glycolysis, many of the 120 non-ribosomal RBP have recently been found to bind mRNA (Hogan et al 2008; Scherrer et al 2010; Tsvetanova et al 2010; Mitchell et al 2013). Thus, affinity purifying Dhh1 under native condition has allowed us to isolate the core PB subcomplexes along with many PB/SG associated proteins known for their role in mRNA binding and translational functions.…”

Section: Resultsmentioning

confidence: 99%

Proteomic analysis of Dhh1 complexes reveals a role for Hsp40 chaperone Ydj1 in yeast P-body assembly

Cary

Vinh

Kuestner

et al. 2015

Preprint

View full text Add to dashboard Cite

P-bodies (PB) are ribonucleoprotein (RNP) complexes that aggregate into cytoplasmic foci when cells are exposed to stress. While the conserved mRNA decay and translational repression machineries are known components of PB, how and why cells assemble RNP complexes into large foci remain unclear. Using mass spectrometry to analyze proteins immunoisolated with the core PB protein Dhh1, we show that a considerable number of proteins contain low-complexity (LC) sequences, similar to proteins highly represented in mammalian RNP granules. We also show that the Hsp40 chaperone Ydj1, which contains an LC domain and controls prion protein aggregation, is required for the formation of Dhh1-GFP foci upon glucose depletion. New classes of proteins that reproducibly co-enrich with Dhh1-GFP during PB induction include proteins involved in nucleotide or amino acid metabolism, glycolysis, tRNA aminoacylation, and protein folding. Many of these proteins have been shown to form foci in response to other stresses. Finally, analysis of RNA associated with Dhh1-GFP shows enrichment of mRNA encoding the PB protein Pat1 and catalytic RNAs along with their associated mitochondrial RNA-binding proteins, suggesting an active role for RNA in PB function. Thus, global characterization of PB composition has uncovered proteins and RNA that are important for PB assembly.

show abstract

“…As an example, protein microarrays have been recently used to test the binding of proteins with a specific RNA in vitro. 43,44 The RNA is fluorescently labeled and hybridized on a protein chip. This method allows the screening of thousands of proteins in less than a day, and relatively small amounts of RNA are required.…”

Section: Rna-centric Approachesmentioning

confidence: 99%

Advances in the characterization of RNA‐binding proteins

et al. 2016

View full text Add to dashboard Cite

From transcription, to transport, storage, and translation, RNA depends on association with different RNA‐binding proteins (RBPs). Methods based on next‐generation sequencing and protein mass‐spectrometry have started to unveil genome‐wide interactions of RBPs but many aspects still remain out of sight. How many of the binding sites identified in high‐throughput screenings are functional? A number of computational methods have been developed to analyze experimental data and to obtain insights into the specificity of protein–RNA interactions. How can theoretical models be exploited to identify RBPs? In addition to oligomeric complexes, protein and RNA molecules can associate into granular assemblies whose physical properties are still poorly understood. What protein features promote granule formation and what effects do these assemblies have on cell function? Here, we describe the newest in silico, in vitro, and in vivo advances in the field of protein–RNA interactions. We also present the challenges that experimental and computational approaches will have to face in future studies. WIREs RNA 2016, 7:793–810. doi: 10.1002/wrna.1378For further resources related to this article, please visit the WIREs website.

show abstract

Environmental Regulation of Prions in Yeast

Cited by 12 publications

References 34 publications

In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles

In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles

Proteomic analysis of Dhh1 complexes reveals a role for Hsp40 chaperone Ydj1 in yeast P-body assembly

Advances in the characterization of RNA‐binding proteins

Contact Info

Product

Resources

About