scholarly journals NMR Analysis of the Hydrogen Bonding Interactions of the RNA-Binding Domains of the Drosophila Sex-Lethal Protein with Target RNA Fragments with Site-Specific [3-15N]Uridine Substitutions

1997 ◽  
Vol 25 (8) ◽  
pp. 1565-1569 ◽  
Author(s):  
I. Kim ◽  
Y. Muto ◽  
M. Inoue ◽  
S. Watanabe ◽  
A. Kitamura ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Rna Binding ◽  
Nmr Analysis ◽  
Site Specific ◽  
Binding Domains ◽  
Hydrogen Bonding Interactions ◽  
Rna Fragments ◽  
Sex Lethal ◽  
Rna Binding Domains ◽  
Target Rna

HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and sex-lethal

Cell ◽  
1991 ◽  
Vol 67 (2) ◽  
pp. 325-333 ◽  
Author(s):  
Aniko Szabo ◽  
Josep Dalmau ◽  
Geoff Manley ◽  
Myrna Rosenfeld ◽  
Ellen Wong ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Domains ◽  
Sex Lethal ◽  
Rna Binding Domains

scholarly journals Interaction of the sex-lethal RNA binding domains with RNA.

1995 ◽  
Vol 14 (18) ◽  
pp. 4530-4539 ◽  
Author(s):  
R. Kanaar ◽  
A. L. Lee ◽  
D. Z. Rudner ◽  
D. E. Wemmer ◽  
D. C. Rio
Keyword(s):  
Rna Binding ◽  
Binding Domains ◽  
Sex Lethal ◽  
Rna Binding Domains

In Caenorhabditis elegans, the RNA-Binding Domains of the Cytoplasmic Polyadenylation Element Binding Protein FOG-1 Are Needed to Regulate Germ Cell Fates

Genetics ◽  
2001 ◽  
Vol 159 (4) ◽  
pp. 1617-1630
Author(s):  
Suk-Won Jin ◽  
Nancy Arno ◽  
Adam Cohen ◽  
Amy Shah ◽  
Qijin Xu ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Germ Cell ◽  
Rna Binding ◽  
Dominant Negative ◽  
Missense Mutations ◽  
Biochemical Tests ◽  
Cell Fates ◽  
Cytoplasmic Polyadenylation ◽  
Binding Domains ◽  
Rna Binding Domains

Abstract FOG-1 controls germ cell fates in the nematode Caenorhabditis elegans. Sequence analyses revealed that FOG-1 is a cytoplasmic polyadenylation element binding (CPEB) protein; similar proteins from other species have been shown to bind messenger RNAs and regulate their translation. Our analyses of fog-1 mutations indicate that each of the three RNA-binding domains of FOG-1 is essential for activity. In addition, biochemical tests show that FOG-1 is capable of binding RNA sequences in the 3′-untranslated region of its own message. Finally, genetic assays reveal that fog-1 functions zygotically, that the small fog-1 transcript has no detectable function, and that missense mutations in fog-1 cause a dominant negative phenotype. This last observation suggests that FOG-1 acts in a complex, or as a multimer, to regulate translation. On the basis of these data, we propose that FOG-1 binds RNA to regulate germ cell fates and that it does so by controlling the translation of its targets. One of these targets might be the fog-1 transcript itself.

Solution Structure of the Complex Formed by the Two N-terminal RNA-binding Domains of Nucleolin and a Pre-rRNA Target

2004 ◽  
Vol 337 (4) ◽  
pp. 799-816 ◽  
Author(s):  
Carina Johansson ◽  
L.David Finger ◽  
Lukas Trantirek ◽  
Thomas D Mueller ◽  
Soyoun Kim ◽  
...  
Keyword(s):  
Solution Structure ◽  
Rna Binding ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals Two RNA-binding Domains Determine the RNA-binding Specificity of Nucleolin

1997 ◽  
Vol 272 (20) ◽  
pp. 13109-13116 ◽  
Author(s):  
Guillaume Serin ◽  
Gérard Joseph ◽  
Laurence Ghisolfi ◽  
Marielle Bauzan ◽  
Monique Erard ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Specificity ◽  
Binding Domains ◽  
Rna Binding Domains
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