scholarly journals A Ribosome Assembly Factor Ebp2p, the Yeast Homolog of EBNA1-Binding Protein 2, Is Involved in the Secretory Response

2008 ◽  
Vol 72 (4) ◽  
pp. 1080-1086 ◽  
Author(s):  
Chihiro HORIGOME ◽  
Takafumi OKADA ◽  
Kana MATSUKI ◽  
Keiko MIZUTA
Keyword(s):  
Binding Protein ◽  
Secretory Response ◽  
Ribosome Assembly ◽  
Assembly Factor ◽  
Yeast Homolog

scholarly journals A yeast homolog of chromatin assembly factor 1 is involved in early ribosome assembly

2001 ◽  
Vol 11 (23) ◽  
pp. 1885-1890 ◽  
Author(s):  
Sigrid Schaper ◽  
Micheline Fromont-Racine ◽  
Patrick Linder ◽  
Jesús de la Cruz ◽  
Abdelkader Namane ◽  
...  
Keyword(s):  
Chromatin Assembly ◽  
Ribosome Assembly ◽  
Chromatin Assembly Factor ◽  
Assembly Factor ◽  
Yeast Homolog

scholarly journals Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2

Structure ◽  
2017 ◽  
Vol 25 (5) ◽  
pp. 762-772.e4 ◽  
Author(s):  
Yu-Hua Lo ◽  
Erin M. Romes ◽  
Monica C. Pillon ◽  
Mack Sobhany ◽  
Robin E. Stanley
Keyword(s):  
Structural Analysis ◽  
Ribosome Assembly ◽  
Assembly Factor

scholarly journals Ribosome assembly factor URB1 contributes to colorectal cancer proliferation through transcriptional activation of ATF4

2020 ◽  
Vol 112 (1) ◽  
pp. 101-116
Author(s):  
Tao Wang ◽  
Lai‐Yuan Li ◽  
Yi‐Feng Chen ◽  
Si‐Wu Fu ◽  
Zhi‐Wei Wu ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Transcriptional Activation ◽  
Ribosome Assembly ◽  
Cancer Proliferation ◽  
Assembly Factor

scholarly journals The Budding Yeast Homolog of the Human EBNA1-binding Protein 2 (Ebp2p) Is an Essential Nucleolar Protein Required for Pre-rRNA Processing

2000 ◽  
Vol 275 (37) ◽  
pp. 28764-28773 ◽  
Author(s):  
Michael D. Huber ◽  
Jessica H. Dworet ◽  
Kathy Shire ◽  
Lori Frappier ◽  
Michael A. McAlear
Keyword(s):  
Budding Yeast ◽  
Binding Protein ◽  
Nucleolar Protein ◽  
Rrna Processing ◽  
Yeast Homolog

scholarly journals Efficient Assembly of Ribosomes Is Inhibited by Deletion ofbipAin Escherichia coli

2015 ◽  
Vol 197 (10) ◽  
pp. 1819-1827 ◽  
Author(s):  
Promisree Choudhury ◽  
Ann M. Flower
Keyword(s):  
Low Temperature ◽  
Modified Nucleosides ◽  
Cold Sensitivity ◽  
23S Rrna ◽  
Ribosome Assembly ◽  
Rrna Processing ◽  
Pseudouridine Synthase ◽  
Assembly Factor ◽  
Cold Sensitive ◽  
And Function

ABSTRACTThe bacterial BipA protein belongs to the EF-G family of translational GTPases and has been postulated to be either a regulatory translation factor or a ribosome assembly factor. To distinguish between these hypotheses, we analyzed the effect ofbipAdeletion on three phenotypes associated with ribosome assembly factors: cold sensitivity, ribosome subunit distribution, and rRNA processing. We demonstrated that a ΔbipAstrain exhibits a cold-sensitive phenotype that is similar to, and synergistic with, that of a strain with a known ribosome assembly factor,deaD. Additionally, thebipAdeletion strain displayed a perturbed ribosome subunit distribution when grown at low temperature, similar to that of adeaDmutant, and again, the double mutant showed additive effects. The primary ribosomal deficiency noted was a decreased level of the 50S subunit and the appearance of a presumed pre-50S particle. Finally, deletion ofbipAresulted in accumulation of pre23S rRNA, as did deletion ofdeaD. We further found that deletion ofrluC, which encodes a pseudouridine synthase that modifies the 23S rRNA at three sites, suppressed all three phenotypes of thebipAmutant, supporting and extending previous findings. Together, these results suggest that BipA is important for the correct and efficient assembly of the 50S subunit of the ribosome at low temperature but when unmodified by RluC, the ribosomes become BipA independent for assembly.IMPORTANCEThe ribosome is the complex ribonucleoprotein machine responsible for protein synthesis in all cells. Although much has been learned about the structure and function of the ribosome, we do not fully understand how it is assembled or the accessory proteins that increase efficiency of biogenesis and function. This study examined one such protein, BipA. Our results indicate that BipA either directly or indirectly enhances the formation of the 50S subunit of the ribosome, particularly at low temperature. In addition, ribosomes contain a large number of modified nucleosides, including pseudouridines. This work demonstrates that the function of BipA is tied to the modification status of the ribosome and may help us understand why these modifications have been retained.

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