scholarly journals The PUMILIO−RNA Interaction:  A Single RNA-Binding Domain Monomer Recognizes a Bipartite Target Sequence†

Biochemistry ◽  
1999 ◽  
Vol 38 (2) ◽  
pp. 596-604 ◽  
Author(s):  
Phillip D. Zamore ◽  
David P. Bartel ◽  
Ruth Lehmann ◽  
James R. Williamson
Keyword(s):  
Rna Binding ◽  
Binding Domain ◽  
Target Sequence ◽  
Rna Binding Domain ◽  
Rna Interaction

scholarly journals LOTUS domain is a novel class of G-rich and G-quadruplex RNA binding domain

2020 ◽  
Vol 48 (16) ◽  
pp. 9262-9272 ◽  
Author(s):  
Deqiang Ding ◽  
Chao Wei ◽  
Kunzhe Dong ◽  
Jiali Liu ◽  
Alexander Stanton ◽  
...  
Keyword(s):  
Rna Binding ◽  
Specific Interaction ◽  
Binding Activity ◽  
Binding Domain ◽  
Binding Property ◽  
Domain Family ◽  
Rna Sequences ◽  
G Quadruplex ◽  
Rna Binding Domain ◽  
Rna Interaction

Abstract LOTUS domains are helix-turn-helix protein folds identified in essential germline proteins and are conserved in prokaryotes and eukaryotes. Despite originally predicted as an RNA binding domain, its molecular binding activity towards RNA and protein is controversial. In particular, the most conserved binding property for the LOTUS domain family remains unknown. Here, we uncovered an unexpected specific interaction of LOTUS domains with G-rich RNA sequences. Intriguingly, LOTUS domains exhibit high affinity to RNA G-quadruplex tertiary structures implicated in diverse cellular processes including piRNA biogenesis. This novel LOTUS domain-RNA interaction is conserved in bacteria, plants and animals, comprising the most ancient binding feature of the LOTUS domain family. By contrast, LOTUS domains do not preferentially interact with DNA G-quadruplexes. We further show that a subset of LOTUS domains display both RNA and protein binding activities. These findings identify the LOTUS domain as a specialized RNA binding domain across phyla and underscore the molecular mechanism underlying the function of LOTUS domain-containing proteins in RNA metabolism and regulation.

scholarly journals RNA Binding Domain of Telomerase Reverse Transcriptase

2001 ◽  
Vol 21 (4) ◽  
pp. 990-1000 ◽  
Author(s):  
Cary K. Lai ◽  
James R. Mitchell ◽  
Kathleen Collins
Keyword(s):  
Catalytic Activity ◽  
Reverse Transcriptase ◽  
Rna Binding ◽  
Binding Domain ◽  
Amino Terminus ◽  
Telomerase Reverse Transcriptase ◽  
Telomerase Rna ◽  
Sequence Motifs ◽  
Rna Binding Domain ◽  
Rna Interaction

ABSTRACT Telomerase is a ribonucleoprotein reverse transcriptase that extends the ends of chromosomes. The two telomerase subunits essential for catalysis in vitro are the telomerase reverse transcriptase (TERT) and the telomerase RNA. Using truncations and site-specific mutations, we identified sequence elements of TERT and telomerase RNA required for catalytic activity and protein-RNA interaction for Tetrahymena thermophila telomerase. We found that the TERT amino and carboxyl termini, although evolutionarily poorly conserved, are nonetheless important for catalytic activity. In contrast, high-affinity telomerase RNA binding requires only a small region in the amino terminus of TERT. Surprisingly, the TERT region necessary and sufficient for telomerase RNA binding is completely separable from the reverse transcriptase motifs. The minimalTetrahymena TERT RNA binding domain contains two sequence motifs with ciliate-specific conservation and one TERT motif with conservation across all species. With human TERT, we demonstrate that a similar region within the TERT amino terminus is essential for human telomerase RNA binding as well. Finally, we defined theTetrahymena telomerase RNA sequences that are essential for TERT interaction. We found that a four-nucleotide region 5′ of the template is critical for TERT binding and that the 5′ end of telomerase RNA is sufficient for TERT binding. Our results reveal at least one evolutionarily conserved molecular mechanism by which the telomerase reverse transcriptase is functionally specialized for obligate use of an internal RNA template.

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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