scholarly journals A nuclear-encoded chloroplast-targeted S1 RNA-binding domain protein affects chloroplast rRNA processing and is crucial for the normal growth ofArabidopsis thaliana

2015 ◽  
Vol 83 (2) ◽  
pp. 277-289 ◽  
Author(s):  
Ji Hoon Han ◽  
Kwanuk Lee ◽  
Kwang Ho Lee ◽  
Sunyo Jung ◽  
Young Jeon ◽  
...  
Keyword(s):  
Rna Binding ◽  
Normal Growth ◽  
Binding Domain ◽  
Rrna Processing ◽  
Ofarabidopsis Thaliana ◽  
Domain Protein ◽  
Rna Binding Domain

scholarly journals Function of the Ski4p (Csl4p) and Ski7p Proteins in 3′-to-5′ Degradation of mRNA

2000 ◽  
Vol 20 (21) ◽  
pp. 8230-8243 ◽  
Author(s):  
Ambro van Hoof ◽  
Robin R. Staples ◽  
Richard E. Baker ◽  
Roy Parker
Keyword(s):  
Point Mutation ◽  
Rna Processing ◽  
Rna Binding ◽  
Mrna Degradation ◽  
Binding Domain ◽  
Rrna Processing ◽  
Loss Of Function ◽  
Partial Loss ◽  
Core Component ◽  
Rna Binding Domain

ABSTRACT One of two general pathways of mRNA decay in the yeastSaccharomyces cerevisiae occurs by deadenylation followed by 3′-to-5′ degradation of the mRNA body. Previous results have shown that this degradation requires components of the exosome and the Ski2p, Ski3p, and Ski8p proteins, which were originally identified due to their superkiller phenotype. In this work, we demonstrate that deletion of the SKI7 gene, which encodes a putative GTPase, also causes a defect in 3′-to-5′ degradation of mRNA. Deletion ofSKI7, like deletion of SKI2, SKI3, or SKI8, does not affect various RNA-processing reactions of the exosome. In addition, we show that a mutation in theSKI4 gene also causes a defect in 3′-to-5′ mRNA degradation. We show that the SKI4 gene is identical to theCSL4 gene, which encodes a core component of the exosome. Interestingly, the ski4-1 allele contains a point mutation resulting in a mutation in the putative RNA binding domain of the Csl4p protein. This point mutation strongly affects mRNA degradation without affecting exosome function in rRNA or snRNA processing, 5′ externally transcribed spacer (ETS) degradation, or viability. In contrast, thecsl4-1 allele of the same gene affects rRNA processing but not 3′-to-5′ mRNA degradation. We identify csl4-1 as resulting from a partial-loss-of-function mutation in the promoter of the CSL4 gene. These data indicate that the distinct functions of the exosome can be separated genetically and suggest that the RNA binding domain of Csl4p may have a specific function in mRNA degradation.

scholarly journals The Scw1 RNA-Binding Domain Protein Regulates Septation and Cell-Wall Structure in Fission Yeast

Genetics ◽  
2002 ◽  
Vol 162 (1) ◽  
pp. 45-58 ◽  
Author(s):  
Jim Karagiannis ◽  
Rena Oulton ◽  
Paul G Young
Keyword(s):  
Cell Wall ◽  
Fission Yeast ◽  
Rna Binding ◽  
Binding Domain ◽  
Negative Regulator ◽  
Wall Structure ◽  
Cell Wall Degrading Enzymes ◽  
Degrading Enzymes ◽  
Domain Protein ◽  
Rna Binding Domain

AbstractLoss of the nonessential RNA-binding domain protein, Scw1, increases resistance to cell-wall-degrading enzymes in fission yeast. Surprisingly, scw1 null mutations also suppress the lethality of mutations (cdc11-136, cdc7-24, cdc14-118, sid1-239, sid2-250, sid3-106, sid4-A1, and mob1-1) at all levels of the sid pathway. This pathway forms part of the septation initiation network (SIN), which regulates the onset of septum formation and ensures the proper coupling of mitosis to cytokinesis. In contrast, scw1- mutations do not suppress ts alleles of the rng genes, cdc12 or cdc15. These mutations also prevent the formation of a septum and in addition block assembly and/or function of the contractile acto-myosin ring. sid mutants exhibit a hyper-sensitivity to cell-wall-degrading enzymes that is suppressed by loss of Scw1. Furthermore, scw1--mediated rescue of sid mutants is abolished in the presence of calcofluor white, a compound that interferes with cell-wall synthesis. These data suggest that Scw1 acts in opposition to the SIN as a negative regulator of cell-wall/septum deposition. Unlike components of the SIN, Scw1 is predominantly a cytoplasmic protein and is not localized to the spindle pole body.

scholarly journals Normal microRNA Maturation and Germ-Line Stem Cell Maintenance Requires Loquacious, a Double-Stranded RNA-Binding Domain Protein

PLoS Biology ◽  
2005 ◽  
Vol 3 (7) ◽  
pp. e236 ◽  
Author(s):  
Klaus Förstemann ◽  
Yukihide Tomari ◽  
Tingting Du ◽  
Vasily V Vagin ◽  
Ahmet M Denli ◽  
...  
Keyword(s):  
Stem Cell ◽  
Rna Binding ◽  
Germ Line ◽  
Binding Domain ◽  
Double Stranded Rna ◽  
Stem Cell Maintenance ◽  
Germ Line Stem Cell ◽  
Domain Protein ◽  
Rna Binding Domain ◽  
Cell Maintenance

scholarly journals Requirement for C-terminal Extension to the RNA Binding Domain for Efficient RNA Binding by Ribosomal Protein L2

2002 ◽  
Vol 66 (3) ◽  
pp. 682-684 ◽  
Author(s):  
Takeshi HAYASHI ◽  
Maino TAHARA ◽  
Kenta IWASAKI ◽  
Yoshiaki KOUZUMA ◽  
Makoto KIMURA
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Domain ◽  
Ribosomal Protein L2 ◽  
Rna Binding Domain

K160 in the RNA‐binding domain of the orf virus virulence factor OV20.0 is critical for its functions in counteracting host antiviral defense

FEBS Letters ◽  
2021 ◽  
Author(s):  
Guan‐Ru Liao ◽  
Yeu‐Yang Tseng ◽  
Ching‐Yu Tseng ◽  
Ying‐Ping Huang ◽  
Ching‐Hsiu Tsai ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Rna Binding ◽  
Binding Domain ◽  
Orf Virus ◽  
Antiviral Defense ◽  
Rna Binding Domain

scholarly journals Characterization of an RNA-binding domain in the bacteriophage phi 29 connector.

1993 ◽  
Vol 268 (27) ◽  
pp. 20198-20204
Author(s):  
L.E. Donate ◽  
J.M. Valpuesta ◽  
C Mier ◽  
F Rojo ◽  
J.L. Carrascosa
Keyword(s):  
Rna Binding ◽  
Binding Domain ◽  
Rna Binding Domain
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