scholarly journals Identification and characterization of srp1, a gene of fission yeast encoding a RNA binding domain and a RS domain typical of SR splicing factors

1998 ◽  
Vol 26 (2) ◽  
pp. 505-511 ◽  
Author(s):  
T. Gross ◽  
K. Richert ◽  
C. Mierke ◽  
M. Lutzelberger ◽  
N. F. Kaufer
Keyword(s):  
Fission Yeast ◽  
Rna Binding ◽  
Binding Domain ◽  
Splicing Factors ◽  
Rna Binding Domain ◽  
Identification And Characterization

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

scholarly journals The identification and characterization of a testis-specific cDNA during spermatogenesis

2006 ◽  
Vol 11 (1) ◽  
Author(s):  
Ying Chen ◽  
Jiarui Hu ◽  
Ping Song ◽  
Wuming Gong
Keyword(s):  
Experimental Validation ◽  
Rna Binding ◽  
Pcr Analysis ◽  
Splicing Factors ◽  
Rt Pcr ◽  
Rich Domain ◽  
Pachytene Spermatocytes ◽  
Identification And Characterization

AbstractUsing bioinformatics and experimental validation, we obtained a cDNA (named srsf) which was exclusively expressed in the mouse testes. RT-PCR analysis showed that srsf mRNA was not expressed in the gonad during the sex determination period or during embryogenesis. In developing mouse tests, srsf expression was first detected on post-natal day 10, reached its highest level on day 23, and then reduced to and remained at a moderate level throughout adulthood. In situ hybridization analysis demonstrated that srsf mRNA was expressed in pachytene spermatocytes and round spermatids in the testes. The predicted protein contains one RNA-binding domain (RBD) and a serine-arginine rich domain (RS), which are characterized by some splicing factors of SR family members. These findings indicate that srsf may play a role during spermatogenesis.

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.

Isolation and Characterization of WHI3, a Size-Control Gene of Saccharomyces cerevisiae

Genetics ◽  
2001 ◽  
Vol 157 (4) ◽  
pp. 1469-1480 ◽  
Author(s):  
R S Nash ◽  
T Volpe ◽  
B Futcher
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Binding ◽  
Size Control ◽  
Binding Domain ◽  
Small Cells ◽  
Yeast Saccharomyces Cerevisiae ◽  
Isolation And Characterization ◽  
Rna Binding Domain ◽  
Mating Factor

Abstract WHI3 is a gene affecting size control and cell cycle in the yeast Saccharomyces cerevisiae. The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start. Whi3 and its partially redundant homolog Whi4 have an RNA-binding domain, and mutagenesis experiments indicate that this RNA-binding domain is essential for Whi3 function. CLN3-1 whi3 cells are extremely small, nearly sterile, and largely nonresponsive to mating factor. Fertility is restored by deletion of CLN2, suggesting that whi3 cells may have abnormally high levels of CLN2 function.

Functional Characterization of the RNA-binding Domain and Motif of the Double-stranded RNA-dependent Protein Kinase DAI (PKR)

1995 ◽  
Vol 249 (1) ◽  
pp. 29-44 ◽  
Author(s):  
Christian Schmedt ◽  
Simon R. Green ◽  
Lisa Manche ◽  
Deborah R. Taylor ◽  
Yuliang Ma ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Rna Binding ◽  
Functional Characterization ◽  
Binding Domain ◽  
Dependent Protein Kinase ◽  
Double Stranded Rna ◽  
Dependent Protein ◽  
Rna Binding Domain
Sign in / Sign up

Export Citation Format

Share Document