scholarly journals Maize Urb2 protein is required for kernel development and vegetative growth by affecting pre-ribosomal RNA processing

2018 ◽  
Vol 218 (3) ◽  
pp. 1233-1246 ◽  
Author(s):  
Hongqiu Wang ◽  
Kai Wang ◽  
Qingguo Du ◽  
Yafei Wang ◽  
Zhiyuan Fu ◽  
...  
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Vegetative Growth ◽  
Kernel Development ◽  
Ribosomal Rna Processing

Adenovirus infection retards ribosomal RNA processing

1989 ◽  
Vol 138 (1) ◽  
pp. 205-207 ◽  
Author(s):  
Susan H. Lawler ◽  
Robert W. Jones ◽  
Brian P. Eliceiri ◽  
George L. Eliceiri
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Adenovirus Infection ◽  
Ribosomal Rna Processing

Developmental expression of fibrillarin and U3 snRNA in Xenopus laevis

Development ◽  
1991 ◽  
Vol 112 (1) ◽  
pp. 317-326
Author(s):  
M. Caizergues-Ferrer ◽  
C. Mathieu ◽  
P. Mariottini ◽  
F. Amalric ◽  
F. Amaldi
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Protein Detection ◽  
Developmental Expression ◽  
Oocyte Growth ◽  
Small Nuclear Ribonucleoprotein ◽  
Hybridization Probes ◽  
Ribosomal Rna Processing ◽  
Protein Components ◽  
Nuclear Ribonucleoprotein

Fibrillarin is one of the protein components that together with U3 snRNA constitute the U3 snRNP, a small nuclear ribonucleoprotein particle involved in ribosomal RNA processing in eucaryotic cells. Using an antifibrillarin antiserum for protein detection and a fibrillarin cDNA and a synthetic oligonucleotide complementary to U3 snRNA as hybridization probes, the expression of these two components has been studied during Xenopus development. Fibrillarin mRNA is accumulated early in oogenesis, like many other messengers, and translated during oocyte growth. Fibrillarin protein is thus progressively accumulated throughout oogenesis to be assembled with U3 snRNA and used for ribosome production in the amplified nucleoli. After fertilization, the amount of U3 snRNA decreases while the maternally accumulated fibrillarin mRNA is maintained and utilized to produce more protein. After the mid-blastula transition, stored fibrillarin is assembled with newly synthesized U3 snRNA and becomes localized in the prenucleolar bodies and reforming nucleoli.

Defect in pre-ribosomal RNA processing is involved in myeloid leukemogenesis

2015 ◽  
Vol 43 (9) ◽  
pp. S78
Author(s):  
Hirotaka Matsui ◽  
Akinori Kanai ◽  
Akiko Nagamachi ◽  
Moe Okuno ◽  
Toshiya Inaba
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Ribosomal Rna Processing

scholarly journals The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast.

1995 ◽  
Vol 9 (20) ◽  
pp. 2470-2481 ◽  
Author(s):  
D Lafontaine ◽  
J Vandenhaute ◽  
D Tollervey
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
18S Rrna ◽  
Ribosomal Rna Processing

scholarly journals Nucleolar Arf Tumor Suppressor Inhibits Ribosomal RNA Processing

2003 ◽  
Vol 11 (2) ◽  
pp. 415-424 ◽  
Author(s):  
Masataka Sugimoto ◽  
Mei-Ling Kuo ◽  
Martine F Roussel ◽  
Charles J Sherr
Keyword(s):  
Tumor Suppressor ◽  
Ribosomal Rna ◽  
Rna Processing ◽  
Ribosomal Rna Processing

scholarly journals A Nucleolar Protein, Ribosomal RNA Processing 1 Homolog B (RRP1B), Enhances the Recruitment of Cellular mRNA in Influenza Virus Transcription

2015 ◽  
Vol 89 (22) ◽  
pp. 11245-11255 ◽  
Author(s):  
Wen-Chi Su ◽  
Shih-Feng Hsu ◽  
Yi-Yuan Lee ◽  
King-Song Jeng ◽  
Michael M. C. Lai
Keyword(s):  
Influenza Virus ◽  
Influenza A Virus ◽  
Ribosomal Rna ◽  
Rna Processing ◽  
Influenza A ◽  
Host Factors ◽  
Viral Rna ◽  
Rna Dependent Rna Polymerase ◽  
Virus Transcription ◽  
Ribosomal Rna Processing

ABSTRACTInfluenza A virus (IAV) undergoes RNA transcription by a unique capped-mRNA-dependent transcription, which is carried out by the viral RNA-dependent RNA polymerase (RdRp), consisting of the viral PA, PB1, and PB2 proteins. However, how the viral RdRp utilizes cellular factors for virus transcription is not clear. Previously, we conducted a genome-wide pooled short hairpin RNA (shRNA) screen to identify host factors important for influenza A virus replication. Ribosomal RNA processing 1 homolog B (RRP1B) was identified as one of the candidates. RRP1B is a nucleolar protein involved in ribosomal biogenesis. Upon IAV infection, part of RRP1B was translocated from the nucleolus to the nucleoplasm, where viral RNA synthesis likely takes place. The depletion of RRP1B significantly reduced IAV mRNA transcription in a minireplicon assay and in virus-infected cells. Furthermore, we showed that RRP1B interacted with PB1 and PB2 of the RdRp and formed a coimmunoprecipitable complex with RdRp. The depletion of RRP1B reduced the amount of capped mRNA in the RdRp complex. Taken together, these findings indicate that RRP1B is a host factor essential for IAV transcription and provide a target for new antivirals.IMPORTANCEInfluenza virus is an important human pathogen that causes significant morbidity and mortality and threatens the human population with epidemics and pandemics every year. Due to the high mutation rate of the virus, antiviral drugs targeting viral proteins might ultimately lose their effectiveness. An alternative strategy that explores the genetic stability of host factors indispensable for influenza virus replication would thus be desirable. Here, we characterized the rRNA processing 1 homolog B (RRP1B) protein as an important cellular factor for influenza A virus transcription. We showed that silencing RRP1B hampered viral RNA-dependent RNA polymerase (RdRp) activity, which is responsible for virus transcription and replication. Furthermore, we reported that RRP1B is crucial for RdRp binding to cellular capped mRNA, which is a critical step of virus transcription. Our study not only provides a deeper understanding of influenza virus-host interplay, but also suggests a potential target for antiviral drug development.

Sign in / Sign up

Export Citation Format

Share Document